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Peptidase

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Structure for peptidase S01.213: coagulation factor XIa

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Pharma

 

PDB Organism Resolution Comment
1ZJD_A Homo sapiens 2.60 Å catalytic domain; complex with Kunitz protease inhibitor domain of protease nexin II
Catalytic residues are shown in ball-and-stick representation: His431 in purple, Asp480 in pink and Ser575 in orange. Kunitz protease inhibitor domain of protease nexin II in grey.
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TERTIARY STRUCTURE DATA
Comment Resolution PDB PDBe SCOP CATH PDBSum Proteopedia Reference
Homo sapiens
complex with ecotin mutant Mer84Arg 2.20 Å 1XX9 1XX9 1XX9 1XX9 1XX9 1XX9 Jin et al., 2005
complex with mutated ecotin 2.91 Å 1XXD 1XXD 1XXD 1XXD 1XXD 1XXD Jin et al., 2005
complex with ecotin mutant (ecotinp) 2.60 Å 1XXF 1XXF 1XXF 1XXF 1XXF 1XXF Jin et al., 2005
catalytic domain Ser434Ala, Thr475Ala, Lys437 mutant; complex with benzamidine 1.96 Å 1ZHM 1ZHM 1ZHM 1ZHM 1ZHM 1ZHM Jin et al., 2005
catalytic domain Ser434Ala, Thr475Ala, Lys505 mutant; complex with benzamidine 2.70 Å 1ZHP 1ZHP 1ZHP 1ZHP 1ZHP 1ZHP Jin et al., 2005
catalytic domain Ser434Ala/Thr475Ala/Cys482Ser/Lys437Ala mutant; complex with benzamidine 1.73 Å 1ZHR 1ZHR 1ZHR 1ZHR 1ZHR 1ZHR Jin et al., 2005
catalytic domain; complex with Kunitz protease inhibitor domain of protease nexin II 2.60 Å 1ZJD 1ZJD 1ZJD 1ZJD 1ZJD 1ZJD Navaneetham et al., 2005
factor xi catalytic domain complexed with 2-guanidino-1-(4- (4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl)ethyl nicotinate 2.50 Å 1ZLR 1ZLR 1ZLR 1ZLR 1ZLR 1ZLR Lazarova et al., 2006
catalytic domain; complex with 4-(guanidinomethyl)-phenylboronic acid 2.00 Å 1ZMJ 1ZMJ 1ZMJ 1ZMJ 1ZMJ 1ZMJ Lazarova et al., 2006
catalytic domain; complex with (R)-1-(4-(4-(hydroxymethyl)-1,3,2- dioxaborolan-2-yl)phenethyl)guanidine 2.25 Å 1ZML 1ZML 1ZML 1ZML 1ZML 1ZML Lazarova et al., 2006
catalytic domain; complex with (r)-1-(4-(4-(hydroxymethyl)-1,3, 2-dioxaborolan-2-yl)phenyl)guanidine 2.05 Å 1ZMN 1ZMN 1ZMN 1ZMN 1ZMN 1ZMN Lazarova et al., 2006
catalytic domain; complex with (S)-2-(3-((R)-1-(4-bromophenyl)ethyl)ureido)-N-((S)-1-((S)-5-guanidino-1-oxo-1-(thiazol-2-yl)pentan-2-ylamino)-3-methyl-1-oxobutan-2-yl)-5-ureidopentanamide 2.25 Å 1ZOM 1ZOM 1ZOM 1ZOM 1ZOM 1ZOM Lin et al., 2006
catalytic domain; complex with 4-methyl-pentanoic acid 1-[4- guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-methyl- p 2.10 Å 1ZPB 1ZPB 1ZPB 1ZPB 1ZPB 1ZPB Deng et al., 2006
catalytic domain; complex with 2-[2-(3-chloro-phenyl)-2-hydroxy- acetylamino]-n-[4-guanidino-1-(thiazole-2-carbonyl)-butyl] 2.60 Å 1ZPC 1ZPC 1ZPC 1ZPC 1ZPC 1ZPC Deng et al., 2006
factor xi catalytic domain complexed with n-((r)-1-(4- bromophenyl)ethyl)urea-asn-val-arg-alpha-ketothiazole 2.50 Å 1ZPZ 1ZPZ 1ZPZ 1ZPZ 1ZPZ 1ZPZ
factor xi complexed with 3-hydroxypropyl 3-(7- amidinonaphthalene-1-carboxamido)benzenesulfonate 2.30 Å 1ZRK 1ZRK 1ZRK 1ZRK 1ZRK 1ZRK
catalytic domain; complex with N-(7-carbamimidoyl-naphthalen-1- yl)-3-hydroxy-2-methyl-benzamide 1.90 Å 1ZSJ 1ZSJ 1ZSJ 1ZSJ 1ZSJ 1ZSJ
catalytic domain; complex with 6-carbamimidoyl-4-(3-hydroxy-2- methyl-benzoylamino)-naphthalene-2-carboxylic acid methyl es 1.90 Å 1ZSK 1ZSK 1ZSK 1ZSK 1ZSK 1ZSK
factor xi complexed with a pyrimidinone inhibitor 2.05 Å 1ZSL 1ZSL 1ZSL 1ZSL 1ZSL 1ZSL
catalytic domain; in complex with 2-(5-benzylamino-2- methylsulfanyl-6-oxo-6h-pyrimidin-1-yl)-n-[4-guanidino-1- (thiazole-2-ca 2.05 Å 1ZTJ 1ZTJ 1ZTJ 1ZTJ 1ZTJ 1ZTJ
catalytic domain; in complex with 2-(5-amino-6-oxo-2-m-tolyl-6h- pyrimidin-1-yl)-n-[4-guanidino-1-(thiazole-2-carbonyl)- butyl 2.50 Å 1ZTK 1ZTK 1ZTK 1ZTK 1ZTK 1ZTK
catalytic domain; complex with n-[4-guanidino-1-(thiazole-2- carbonyl)-butyl]-2-6-oxo-5-[(quinolin-8-ylmethyl)-amino]- 2-m 2.60 Å 1ZTL 1ZTL 1ZTL 1ZTL 1ZTL 1ZTL
precursor 2.87 Å 2F83 2F83 2F83 2F83 2F83 2F83 Papagrigoriou et al., 2006
catalytic domain; complex with N~2~-(aminocarbonyl)-N~1~-4-[amino(imino)methyl]amino-1-[hydroxy(1,3-thiazol-2-yl)methyl]butylvalinamide 2.00 Å 2FDA 2FDA 2FDA 2FDA 2FDA 2FDA Deng et al., 2006
mature  peptidase 0.00 Å 2J8J 2J8J 2J8J 2J8J 2J8J 2J8J Samuel et al., 2007
mature  peptidase 0.00 Å 2J8L 2J8L 2J8L 2J8L 2J8L 2J8L Samuel et al., 2007
complex with clavatadine A 1.60 Å 3BG8 3BG8 3BG8 3BG8 3BG8 3BG8 Buchanan et al., 2008
mature  peptidase 1.80 Å 3SOR 3SOR 3SOR 3SOR 3SOR 3SOR Fradera et al., 2012
mature  peptidase 2.58 Å 3SOS 3SOS 3SOS 3SOS 3SOS 3SOS Fradera et al., 2012
mature  peptidase 2.00 Å 4CR5 4CR5 4CR5 4CR5 4CR5 4CR5 Fjellstrom et al., 2015
mature  peptidase 1.70 Å 4CR9 4CR9 4CR9 4CR9 4CR9 4CR9 Fjellstrom et al., 2015
mature  peptidase 1.80 Å 4CRA 4CRA 4CRA 4CRA 4CRA 4CRA Fjellstrom et al., 2015
mature  peptidase 1.85 Å 4CRB 4CRB 4CRB 4CRB 4CRB 4CRB Fjellstrom et al., 2015
mature  peptidase 1.60 Å 4CRC 4CRC 4CRC 4CRC 4CRC 4CRC Fjellstrom et al., 2015
mature  peptidase 2.10 Å 4CRD 4CRD 4CRD 4CRD 4CRD 4CRD Fjellstrom et al., 2015
mature  peptidase 1.73 Å 4CRE 4CRE 4CRE 4CRE 4CRE 4CRE Fjellstrom et al., 2015
mature  peptidase 2.30 Å 4CRF 4CRF 4CRF 4CRF 4CRF 4CRF Fjellstrom et al., 2015
mature  peptidase 1.25 Å 4CRG 4CRG 4CRG 4CRG 4CRG 4CRG Fjellstrom et al., 2015
human fxia in complex with small molecule inhibitors. 1.77 Å 4D76 4D76 4D76 4D76 4D76 4D76
human fxia in complex with small molecule inhibitors. 1.62 Å 4D7F 4D7F 4D7F 4D7F 4D7F 4D7F
human fxia in complex with small molecule inhibitors. 2.33 Å 4D7G 4D7G 4D7G 4D7G 4D7G 4D7G
mature  peptidase 2.80 Å 4NA7 4NA7 4NA7 4NA7 4NA7 4NA7 Quan et al., 2014
mature  peptidase 2.30 Å 4NA8 4NA8 4NA8 4NA8 4NA8 4NA8 Quan et al., 2014
mature  peptidase 1.85 Å 4TY6 4TY6 4TY6 4TY6 4TY6 4TY6 Hangeland et al., 2014
mature  peptidase 2.09 Å 4TY7 4TY7 4TY7 4TY7 4TY7 4TY7 Hangeland et al., 2014
mature  peptidase 2.60 Å 4WXI 4WXI 4WXI 4WXI 4WXI 4WXI Corte et al., 2015
mature  peptidase 2.40 Å 4X6M 4X6M 4X6M 4X6M 4X6M 4X6M Pinto et al., 2015
mature  peptidase 2.10 Å 4X6N 4X6N 4X6N 4X6N 4X6N 4X6N Pinto et al., 2015
mature  peptidase 2.10 Å 4X6O 4X6O 4X6O 4X6O 4X6O 4X6O Pinto et al., 2015
mature  peptidase 1.93 Å 4X6P 4X6P 4X6P 4X6P 4X6P 4X6P Pinto et al., 2015
mature  peptidase 1.90 Å 4Y8X 4Y8X 4Y8X 4Y8X 4Y8X 4Y8X
mature  peptidase 2.60 Å 4Y8Y 4Y8Y 4Y8Y 4Y8Y 4Y8Y 4Y8Y
mature  peptidase 2.20 Å 4Y8Z 4Y8Z 4Y8Z 4Y8Z 4Y8Z 4Y8Z
mature  peptidase 2.08 Å 5E2O 5E2O 5E2O 5E2O 5E2O 5E2O Smith et al., 2016
mature  peptidase 2.11 Å 5E2P 5E2P 5E2P 5E2P 5E2P 5E2P Smith et al., 2016
human plasma coagulation fxi with peptide lp2 ***caveat 5eod lys a 8 has wrong chirality at atom ca nag a 901 has wrong ***caveat 2 5eod chirality at atom c1 nag a 902 has wrong chirality at atom ***caveat 3 5eod c1 3.10 Å 5EOD 5EOD 5EOD 5EOD 5EOD 5EOD
human plasma coagulation factor xi in complex with peptide p39 ***caveat 5eok glu a 323 has wrong chirality at atom ca nag a 701 has wrong ***caveat 2 5eok chirality at atom c1 nag a 703 has wrong chirality at atom ***caveat 3 5eok c1 2.80 Å 5EOK 5EOK 5EOK 5EOK 5EOK 5EOK
in complex with the inhibitor 4-(aminomethyl)-~n- [(1~s)-1-[4-(3-oxidanyl-1~h-indazol-5-yl)pyridin-2-yl]-2-phenyl- ethyl]cyclohexane-1-carboxamide 2.30 Å 5EXL 5EXL 5EXL 5EXL 5EXL 5EXL
complex with the inhibitor methyl ~n-[4-[2-[(1~s)-1-[[4-(aminomethyl)cyclohexyl]carbonylamino]-2-phenyl-ethyl]pyridin-4- yl]phenyl]carbamate 2.09 Å 5EXM 5EXM 5EXM 5EXM 5EXM 5EXM
Cys500Ser [Cys122Ser] mutant; complex with the inhibitor methyl ~n- [4-[2-[(1~s)-1-[[(~e)-3-[5-chloranyl-2-(1,2,3,4-tetrazol-1-yl) phenyl]prop-2-enoyl]amino]-2-phenyl-ethyl]pyridin-4- yl]phenyl]carbamate 1.49 Å 5EXN 5EXN 5EXN 5EXN 5EXN 5EXN
human recombinant coagulation fxi in complex with a peptide derived from human high molecular weight kininogen (hkp) 2.85 Å 5I25 5I25 5I25 5I25 5I25 5I25
complex with the inhibitor methyl [(7s)-7-((2e)-3-[5- chloro-2-(1h-tetrazol-1-yl)phenyl]prop-2-enoylamino)-2-oxo-1,2,3,4, 5,6,7,9-octahydro-11,8-(azeno)-1,9-benzodiazacyclotridecin-14- yl]carbamate 2.12 Å 5Q0D 5Q0D 5Q0D 5Q0D 5Q0D 5Q0D
complex with the inhibitor methyl [(4s,8s)-8-((2e)-3- [5-chloro-2-(1h-tetrazol-1-yl)phenyl]prop-2-enoylamino)-4-methyl-2- oxo-1,3,4,5,6,7,8,10-octahydro-2h-12,9-(azeno)-1,10- benzodiazacyclotetradecin-15-yl]carbamate 2.12 Å 5Q0E 5Q0E 5Q0E 5Q0E 5Q0E 5Q0E
complex with the inhibitor methyl [(4r,5e,8s)-8-((2e)- 3-[5-chloro-2-(1h-tetrazol-1-yl)phenyl]prop-2-enoylamino)-4-methyl- 2-oxo-1,3,4,7,8,10-hexahydro-2h-12,9-(azeno)-1,10- benzodiazacyclotetradecin-15-yl]carbamate 2.12 Å 5Q0F 5Q0F 5Q0F 5Q0F 5Q0F 5Q0F
complex with the inhibitor methyl [(3r,7s)-7-((2e)-3- [5-chloro-2-(1h-tetrazol-1-yl)phenyl]prop-2-enoylamino)-3-ethyl-2- oxo-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9- benzodiazacyclotridecin-14-yl]carbamate 2.60 Å 5Q0G 5Q0G 5Q0G 5Q0G 5Q0G 5Q0G
complex with the inhibitor methyl [(4r,5e,8s)-11-chloro-8-[(2,6-difluoro-4-methylbenzene-1-carbonyl)amino]-4-methyl-2-oxo-1, 3,4,7,8,10-hexahydro-2h-12,9-(azeno)-1,10-benzodiazacyclotetradecin- 15-yl]carbamate 2.50 Å 5Q0H 5Q0H 5Q0H 5Q0H 5Q0H 5Q0H
complex with the inhibitor 4-[[(2~s,3~r)-1-[(~e)- 3-[5-chloranyl-2-(1,2,3,4-tetrazol-1-yl)phenyl]prop-2-enoyl]-3- phenyl-pyrrolidin-2-yl]carbonylamino]benzoic acid 2.64 Å 5QCK 5QCK 5QCK 5QCK 5QCK 5QCK
complex with the inhibitor 4-[[(1~s)-2-[(~e)-3-[5- chloranyl-2-(1,2,3,4-tetrazol-1-yl)phenyl]prop-2-enoyl]-3,4-dihydro- 1~h-isoquinolin-1-yl]carbonylamino]benzoic acid 2.11 Å 5QCL 5QCL 5QCL 5QCL 5QCL 5QCL
factor xia in complex with the inhibitor methyl ~n-[4-[[(1~s)-2- [(~e)-3-[3-chloranyl-2-fluoranyl-6-(1,2,3,4-tetrazol-1-yl) phenyl]prop-2-enoyl]-3,4-dihydro-1~h-isoquinolin-1- yl]carbonylamino]phenyl]carbamate 2.20 Å 5QCM 5QCM 5QCM 5QCM 5QCM 5QCM
complex with the inhibitor 4-[[(1~s)-2-[(~e)-3-[5- chloranyl-2-(1,2,3,4-tetrazol-1-yl)phenyl]prop-2-enoyl]-5-[(3~s)-3-ethoxycarbonylpiperidin-1-yl]carbonyl-3,4-dihydro-1~h-isoquinolin- 1-yl]carbonylamino]benzoic acid 2.30 Å 5QCN 5QCN 5QCN 5QCN 5QCN 5QCN
complex with the inhibitor ((15s)-18-chloro- 15-(((2e)- 3-(5-chloro-2-(1h-tetrazol-1-yl)phenyl)-2- propenoyl)amino)-17,19- diazatricyclo[14.2.1.0~2,7~]nonadeca-1(18),2,4,6,16(19)-pentaen-5- yl)carbamate 1.55 Å 5TKS 5TKS 5TKS 5TKS 5TKS 5TKS
complex with the inhibitor methyl ((12e,15s)-15-(((2e)- 3-(5-chloro-2-(1h-tetrazol-1-yl)phenyl)-2-propenoyl)amino)-9-oxo-8, 17,19-triazatricyclo[14.2.1.0~2,7~]nonadeca-1(18),2,4,6,12,16(19)- hexaen-5-yl)carbamate 2.12 Å 5TKT 5TKT 5TKT 5TKT 5TKT 5TKT
complex with the inhibitor methyl ((15s)-15-(((2e)-3-(5-chloro-2-(1h-tetrazol-1-yl)phenyl)-2-propenoyl)amino)-9-oxo-8,17,19- triazatricyclo[14.2.1.0~2,7~]nonadeca-1(18),2,4,6,16(19)-pentaen-5- yl)carbamate 2.12 Å 5TKU 5TKU 5TKU 5TKU 5TKU 5TKU
complex with the inhibitor methyl [(11s)-11-((2e)-3-[5-chloro-2-(1h-tetrazol-1-yl)phenyl]prop-2-enoylamino)-6-fluoro-2-oxo-1,3,4,10,11,13-hexahydro-2h-5,9:15,12-di(azeno)-1,13- benzodiazacycloheptadecin-18-yl]carbamate 2.35 Å 5WB6 5WB6 5WB6 5WB6 5WB6 5WB6
fxia antibody complex 1.80 Å 6AOD 6AOD 6AOD 6AOD 6AOD 6AOD
complex with the inhibitor methyl (4-6-[(1s)-2-[(3r)-1-acetylpiperidin-3-yl]-1-((2e)-3-[5-chloro-2- (1h-tetrazol-1-yl) phenyl]prop-2-enoylamino)ethyl]-3-chloropyridazin-4-ylphenyl) carbamate 2.35 Å 6C0S 6C0S 6C0S 6C0S 6C0S 6C0S
allosteric activation of human prekallikrein by apple domain disc rotation 2.60 Å 6I58 6I58 6I58 6I58 6I58 6I58
catalytic domain; complex with fab-portion of maa868 2.04 Å 6R8X 6R8X 6R8X 6R8X 6R8X 6R8X

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