Structure for peptidase M24.001: methionyl aminopeptidase 1 (Escherichia-type)

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Pharma

 

PDB Organism Resolution Comment
1MAT Escherichia coli 2.40 Å mature
The catalytic cobalt ions are shown as light grey CPK spheres. The cobalt ligands are shown in ball-and-stick representation: Asp97 and Asp108 in light pink, His171 in purple, and Glu204 and Glu235 in dark blue. The catalytic His79 is shown in ball-and-stick representation in purple.
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TERTIARY STRUCTURE DATA
Comment Resolution PDB PDBe SCOP CATH PDBSum Proteopedia Reference
Escherichia coli
complex with methionine 1.80 Å 1C21 1C21 1C21 1C21 1C21 1C21 Lowther et al., 1999
complex with trifluoromethionine 1.75 Å 1C22 1C22 1C22 1C22 1C22 1C22 Lowther et al., 1999
complex with methionine phosphonate 2.00 Å 1C23 1C23 1C23 1C23 1C23 1C23 Lowther et al., 1999
complex with methionine phosphinate 1.70 Å 1C24 1C24 1C24 1C24 1C24 1C24 Lowther et al., 1999
complex with norleucine phosphonate 1.95 Å 1C27 1C27 1C27 1C27 1C27 1C27 Lowther et al., 1999
mature  peptidase 2.40 Å 1MAT 1MAT 1MAT 1MAT 1MAT 1MAT Roderick & Matthews, 1993
complex with 5-(2-chlorophenyl)furan-2-carboxylic acid 1.52 Å 1XNZ 1XNZ 1XNZ 1XNZ 1XNZ 1XNZ Ye et al., 2004
mature  peptidase 1.60 Å 1YVM 1YVM 1YVM 1YVM 1YVM 1YVM Schiffmann et al., 2005
mature  peptidase 1.70 Å 2BB7 2BB7 2BB7 2BB7 2BB7 2BB7 Huang et al., 2006
complex with 5-(2-(trifluoromethyl)phenyl)furan-2- carboxylic acid 1.60 Å 2EVC 2EVC 2EVC 2EVC 2EVC 2EVC Xie et al., 2006
complex with 5-(2,5-dichlorophenyl)furan-2-carboxylic acid 1.70 Å 2EVM 2EVM 2EVM 2EVM 2EVM 2EVM Xie et al., 2006
complex with n-cyclopentyl-n-(thiazol-2-yl)oxalamide 1.70 Å 2EVO 2EVO 2EVO 2EVO 2EVO 2EVO Xie et al., 2006
novel bacterial methionine aminopeptidase inhibitors 1.28 Å 2GG0 2GG0 2GG0 2GG0 2GG0 2GG0 Evdokimov et al., 2007
novel bacterial methionine aminopeptidase inhibitors 1.00 Å 2GG2 2GG2 2GG2 2GG2 2GG2 2GG2 Evdokimov et al., 2007
novel bacterial methionine aminopeptidase inhibitors 1.45 Å 2GG3 2GG3 2GG3 2GG3 2GG3 2GG3 Evdokimov et al., 2007
novel bacterial methionine aminopeptidase inhibitors 2.12 Å 2GG5 2GG5 2GG5 2GG5 2GG5 2GG5 Evdokimov et al., 2007
novel bacterial methionine aminopeptidase inhibitors 1.12 Å 2GG7 2GG7 2GG7 2GG7 2GG7 2GG7 Evdokimov et al., 2007
novel bacterial methionine aminopeptidase inhibitors 1.80 Å 2GG8 2GG8 2GG8 2GG8 2GG8 2GG8 Evdokimov et al., 2007
novel bacterial methionine aminopeptidase inhibitors 1.05 Å 2GG9 2GG9 2GG9 2GG9 2GG9 2GG9 Evdokimov et al., 2007
novel bacterial methionine aminopeptidase inhibitors 2.13 Å 2GGB 2GGB 2GGB 2GGB 2GGB 2GGB Evdokimov et al., 2007
novel bacterial methionine aminopeptidase inhibitors 1.00 Å 2GGC 2GGC 2GGC 2GGC 2GGC 2GGC Evdokimov et al., 2007
structural basis of catalysis by mononuclear methionine aminopeptidase 2.00 Å 2GTX 2GTX 2GTX 2GTX 2GTX 2GTX Ye et al., 2006
complex with nlep, 1: 0.5, di-metalated 1.80 Å 2GU4 2GU4 2GU4 2GU4 2GU4 2GU4 Ye et al., 2006
complex with nlep, 1: 1, di-metalated 1.60 Å 2GU5 2GU5 2GU5 2GU5 2GU5 2GU5 Ye et al., 2006
complex with nlep, 1: 2, di-metalated 1.70 Å 2GU6 2GU6 2GU6 2GU6 2GU6 2GU6 Ye et al., 2006
e. coli methionine aminopeptidase unliganded, 1:0.5 2.00 Å 2GU7 2GU7 2GU7 2GU7 2GU7 2GU7 Ye et al., 2006
mature  peptidase 1.90 Å 2MAT 2MAT 2MAT 2MAT 2MAT 2MAT Lowther et al., 1999
complex with inhibitor YE7 0.00 Å 2P98 2P98 2P98 2P98 2P98 2P98 Huang et al., 2007
complex with inhibitor YE6 0.00 Å 2P99 2P99 2P99 2P99 2P99 2P99 Huang et al., 2007
complex with inhibitor YE6 0.00 Å 2P9A 2P9A 2P9A 2P9A 2P9A 2P9A Huang et al., 2007
e. coli methionine aminopeptidase mn-form with inhibitor b23 1.90 Å 2Q92 2Q92 2Q92 2Q92 2Q92 2Q92 Ma et al., 2007
e. coli methionine aminopeptidase mn-form with inhibitor b21 1.60 Å 2Q93 2Q93 2Q93 2Q93 2Q93 2Q93 Ma et al., 2007
e. coli methionine aminopeptidase mn-form with inhibitor a04 1.63 Å 2Q94 2Q94 2Q94 2Q94 2Q94 2Q94 Ma et al., 2007
e. coli methionine aminopeptidase mn-form with inhibitor a05 1.70 Å 2Q95 2Q95 2Q95 2Q95 2Q95 2Q95 Ma et al., 2007
e. coli methionine aminopeptidase mn-form with inhibitor a18 1.60 Å 2Q96 2Q96 2Q96 2Q96 2Q96 2Q96 Ma et al., 2007
e. coli methionine aminopeptidase with fe inhibitor w29 2.20 Å 3D27 3D27 3D27 3D27 3D27 3D27 Wang et al., 2008
Arg175Gln mutant; complex with amino-hydroxyheptanyl-Ala-Leu-Val-Phe 2.00 Å 3MAT 3MAT 3MAT 3MAT 3MAT 3MAT Lowther et al., 1999
x-ray structures of oxazole hydroxamate ecmetap-mn complexes 1.46 Å 4A6V 4A6V 4A6V 4A6V 4A6V 4A6V
x-ray structures of oxazole hydroxamate ecmetap-mn complexes 1.46 Å 4A6W 4A6W 4A6W 4A6W 4A6W 4A6W
His79Ala mutant 2.00 Å 4MAT 4MAT 4MAT 4MAT 4MAT 4MAT Lowther et al., 1999
e. coli methionine aminopeptidase in complex with inhibitor 7-methoxy-2-methylen-3,4-dihydronaphthalen-1(2h)-one 1.54 Å 4PNC 4PNC 4PNC 4PNC 4PNC 4PNC
novel inhibitors of bacterial methionine aminopeptidase with broad- spectrum biochemical activity 1.43 Å 4Z7M 4Z7M 4Z7M 4Z7M 4Z7M 4Z7M
e. coli methionine aminopeptidase crystal structure fitted into the cryo-em density map of e. coli 70s ribosome in complex with methionine aminopeptidase 11.80 Å 6IZ7 6IZ7 6IZ7 6IZ7 6IZ7 6IZ7
crystal structure of e. coli peptide deformylase and methionine aminopeptidase fitted into the cryo-em density map of the complex 11.80 Å 6IZI 6IZI 6IZI 6IZI 6IZI 6IZI
crystal structure of e. coli methionine aminopeptidase enzyme and chaperone trigger factor fitted into the cryo-em density map of the complex 14.20 Å 6J0A 6J0A 6J0A 6J0A 6J0A 6J0A
Pseudomonas aeruginosa
pseudomonas aeruginosa metap, in mn form 1.80 Å 4FO7 4FO7 4FO7 4FO7 4FO7 4FO7
pseudomonas aeruginosa metap with met, in mn form 1.90 Å 4FO8 4FO8 4FO8 4FO8 4FO8 4FO8
pseudomonas aeruginosa metap t2n mutant, in mn form 2.20 Å 4JUQ 4JUQ 4JUQ 4JUQ 4JUQ 4JUQ
Rickettsia prowazekii
mature  peptidase 2.00 Å 3MR1 3MR1 3MR1 3MR1 3MR1 3MR1
mature  peptidase 1.70 Å 3MX6 3MX6 3MX6 3MX6 3MX6 3MX6