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1QXY

Crystal structure of S. aureus methionine aminopeptidase in complex with a ketoheterocycle 618

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004239molecular_functioninitiator methionyl aminopeptidase activity
A0006508biological_processproteolysis
A0008235molecular_functionmetalloexopeptidase activity
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 1001
ChainResidue
AASP104
AHIS168
AGLU202
AGLU233
ACO1002
AM2C3001

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 1002
ChainResidue
ACO1001
AM2C3001
AASP93
AASP104
AGLU233

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 1003
ChainResidue
AHIS168
AHIS175
AM2C3001
AHOH3148
AHOH3172

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 2001
ChainResidue
AHIS151
ALYS160
AVAL161
ASER210
AHOH3125

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE M2C A 3001
ChainResidue
APRO56
AGLU60
AALA75
AASP93
AASP104
AHIS168
ALEU174
AHIS175
AGLU202
APHE204
AGLU233
ACO1001
ACO1002
ACO1003
AHOH3035
AHOH3148
AHOH3172
AHOH3293

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322
ChainResidueDetails
AHIS76
AASP93
AASP104
AHIS168
AHIS175
AGLU202
AGLU233

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AHIS180
AGLU202

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AHIS76
AGLY106
AGLU202

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU202

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PDB entries from 2024-07-17

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