Structure for peptidase M01.004: leukotriene A4 hydrolase

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

 

PDB Organism Resolution Comment
1HS6_A Homo sapiens 1.95 Å complex with bestatin
The catalytic zinc is shown as a light grey CPK sphere. The zinc ligands are shown in ball-and-stick representation: His295 and His299 in purple, and Glu318 in dark blue. The catalytic Glu296 is also shown in ball-and-stick representation in dark blue. Bound bestatin is shown in grey in ball-and-stick representation.
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TERTIARY STRUCTURE DATA
Comment Resolution PDB PDBe SCOP CATH PDBSum Proteopedia Reference
Homo sapiens
Asp375Asn mutant 2.20 Å 1GW6 1GW6 1GW6 1GW6 1GW6 1GW6 Rudberg et al., 2002
Glu271Gln mutant 2.10 Å 1H19 1H19 1H19 1H19 1H19 1H19 Rudberg et al., 2002
complex with bestatin 1.95 Å 1HS6 1HS6 1HS6 1HS6 1HS6 1HS6 Thunnissen et al., 2001
structure of [r563a] leukotriene a4 hydrolase 2.30 Å 1SQM 1SQM 1SQM 1SQM 1SQM 1SQM Rudberg et al., 2004
leukotriene a4 hydrolase complexed with inhibitor rb3041 1.89 Å 2R59 2R59 2R59 2R59 2R59 2R59 Thunnissen et al., 2001
mature  peptidase 1.80 Å 2VJ8 2VJ8 2VJ8 2VJ8 2VJ8 2VJ8 Thunnissen et al., 2002
leukotriene a4 hydrolase complexed with inhibitor rb3040 1.81 Å 3B7R 3B7R 3B7R 3B7R 3B7R 3B7R Thunnissen et al., 2001
Glu296Gln mutant; complex with RSR substrate 1.47 Å 3B7S 3B7S 3B7S 3B7S 3B7S 3B7S Thunnissen et al., 2001
Glu296Gln mutant; complex with Arg-Ala-Arg substrate 2.30 Å 3B7T 3B7T 3B7T 3B7T 3B7T 3B7T Thunnissen et al., 2001
leukotriene a4 hydrolase complexed with kelatorphan 1.90 Å 3B7U 3B7U 3B7U 3B7U 3B7U 3B7U Thunnissen et al., 2001
complex with 2-amino-N-[4-(phenylmethoxy)phenyl]-acetamide 1.80 Å 3CHO 3CHO 3CHO 3CHO 3CHO 3CHO Kirkland et al., 2008
complex with (3S)-3-amino-4-oxo-4-[(4-phenylmethoxyphenyl) amino]butanoic acid 2.10 Å 3CHP 3CHP 3CHP 3CHP 3CHP 3CHP Kirkland et al., 2008
complex with N5-[4-(phenylmethoxy)phenyl]-L-glutamine 2.09 Å 3CHQ 3CHQ 3CHQ 3CHQ 3CHQ 3CHQ Kirkland et al., 2008
complex with 4-amino-N-[4-(phenylmethoxy)phenyl]-butanamide 2.20 Å 3CHR 3CHR 3CHR 3CHR 3CHR 3CHR Kirkland et al., 2008
complex with (2S)-2-amino-5-[[4-[(2S)-2-hydroxy-2-phenyl- ethoxy]phenyl]amino]-5-oxo-pentanoic acid 2.55 Å 3CHS 3CHS 3CHS 3CHS 3CHS 3CHS Kirkland et al., 2008
mature  peptidase 1.63 Å 3FH5 3FH5 3FH5 3FH5 3FH5 3FH5 Sandanayaka et al., 2010
mature  peptidase 2.05 Å 3FH7 3FH7 3FH7 3FH7 3FH7 3FH7 Sandanayaka et al., 2010
mature  peptidase 1.67 Å 3FH8 3FH8 3FH8 3FH8 3FH8 3FH8 Sandanayaka et al., 2010
mature  peptidase 2.16 Å 3FHE 3FHE 3FHE 3FHE 3FHE 3FHE Sandanayaka et al., 2010
mature  peptidase 2.33 Å 3FTS 3FTS 3FTS 3FTS 3FTS 3FTS Davies et al., 2009
mature  peptidase 1.90 Å 3FTU 3FTU 3FTU 3FTU 3FTU 3FTU Davies et al., 2009
mature  peptidase 1.70 Å 3FTV 3FTV 3FTV 3FTV 3FTV 3FTV Davies et al., 2009
mature  peptidase 1.85 Å 3FTW 3FTW 3FTW 3FTW 3FTW 3FTW Davies et al., 2009
mature  peptidase 1.96 Å 3FTX 3FTX 3FTX 3FTX 3FTX 3FTX Davies et al., 2009
mature  peptidase 2.15 Å 3FTY 3FTY 3FTY 3FTY 3FTY 3FTY Davies et al., 2009
mature  peptidase 2.00 Å 3FTZ 3FTZ 3FTZ 3FTZ 3FTZ 3FTZ Sandanayaka et al., 2010
mature  peptidase 1.80 Å 3FU0 3FU0 3FU0 3FU0 3FU0 3FU0 Davies et al., 2009
mature  peptidase 2.00 Å 3FU3 3FU3 3FU3 3FU3 3FU3 3FU3 Davies et al., 2009
mature  peptidase 2.30 Å 3FU5 3FU5 3FU5 3FU5 3FU5 3FU5 Davies et al., 2009
mature  peptidase 2.05 Å 3FU6 3FU6 3FU6 3FU6 3FU6 3FU6 Davies et al., 2009
mature  peptidase 2.20 Å 3FUD 3FUD 3FUD 3FUD 3FUD 3FUD Davies et al., 2009
mature  peptidase 2.38 Å 3FUE 3FUE 3FUE 3FUE 3FUE 3FUE Davies et al., 2009
mature  peptidase 2.60 Å 3FUF 3FUF 3FUF 3FUF 3FUF 3FUF Davies et al., 2009
mature  peptidase 1.80 Å 3FUH 3FUH 3FUH 3FUH 3FUH 3FUH Davies et al., 2009
mature  peptidase 2.20 Å 3FUI 3FUI 3FUI 3FUI 3FUI 3FUI Davies et al., 2009
mature  peptidase 1.90 Å 3FUJ 3FUJ 3FUJ 3FUJ 3FUJ 3FUJ Davies et al., 2009
mature  peptidase 1.95 Å 3FUK 3FUK 3FUK 3FUK 3FUK 3FUK Davies et al., 2009
mature  peptidase 2.39 Å 3FUL 3FUL 3FUL 3FUL 3FUL 3FUL Sandanayaka et al., 2010
mature  peptidase 2.15 Å 3FUM 3FUM 3FUM 3FUM 3FUM 3FUM Davies et al., 2009
mature  peptidase 1.58 Å 3FUN 3FUN 3FUN 3FUN 3FUN 3FUN Davies et al., 2009
mature  peptidase 1.25 Å 3U9W 3U9W 3U9W 3U9W 3U9W 3U9W
mature  peptidase 2.02 Å 4DPR 4DPR 4DPR 4DPR 4DPR 4DPR
mature  peptidase 1.65 Å 4L2L 4L2L 4L2L 4L2L 4L2L 4L2L Stsiapanava et al., 2014
mature  peptidase 1.62 Å 4MKT 4MKT 4MKT 4MKT 4MKT 4MKT Stsiapanava et al., 2014
mature  peptidase 1.72 Å 4MS6 4MS6 4MS6 4MS6 4MS6 4MS6 Stsiapanava et al., 2014
mature  peptidase 1.66 Å 4R7L 4R7L 4R7L 4R7L 4R7L 4R7L
mature  peptidase 1.93 Å 4RSY 4RSY 4RSY 4RSY 4RSY 4RSY
mature  peptidase 1.93 Å 4RVB 4RVB 4RVB 4RVB 4RVB 4RVB
mature  peptidase 1.86 Å 5AEN 5AEN 5AEN 5AEN 5AEN 5AEN Moser et al., 2015
complex with inhibitor 4az 2.03 Å 5BPP 5BPP 5BPP 5BPP 5BPP 5BPP
apo form 2.05 Å 5FWQ 5FWQ 5FWQ 5FWQ 5FWQ 5FWQ
crystal structure of lta4h bound to a selective inhibitor against ltb4generation 2.30 Å 5N3W 5N3W 5N3W 5N3W 5N3W 5N3W
lta4h Glu271Ala mutant; complex with lta4 (crystal form I) 1.50 Å 5NI2 5NI2 5NI2 5NI2 5NI2 5NI2
lta4h Glu271Ala mutant; complex with lta4 (crystal form II) 1.90 Å 5NI4 5NI4 5NI4 5NI4 5NI4 5NI4
Asp375Asn mutant; complex with lta4 1.54 Å 5NI6 5NI6 5NI6 5NI6 5NI6 5NI6
crystal structure of human lta4h mutant d375n in open conformation (crystal form i) 1.76 Å 5NIA 5NIA 5NIA 5NIA 5NIA 5NIA
crystal structure of human lta4h mutant d375n in open conformation (crystal form ii) 1.57 Å 5NID 5NID 5NID 5NID 5NID 5NID
crystal structure of human lta4h mutant r563a in open conformation 2.60 Å 5NIE 5NIE 5NIE 5NIE 5NIE 5NIE
lta4 hydrolase (e297q) mutant in complex with pro-gly-pro peptide 1.84 Å 6ENB 6ENB 6ENB 6ENB 6ENB 6ENB
lta4 hydrolase in complex with compound11 1.95 Å 6ENC 6ENC 6ENC 6ENC 6ENC 6ENC
lta4 hydrolase in complex with compound15 2.24 Å 6END 6END 6END 6END 6END 6END
Xenopus laevis
complex with inhibitor bestatin 2.26 Å 4GAA 4GAA 4GAA 4GAA 4GAA 4GAA