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1YVM

E. coli Methionine Aminopeptidase in complex with thiabendazole

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004239molecular_functioninitiator methionyl aminopeptidase activity
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008198molecular_functionferrous iron binding
A0008235molecular_functionmetalloexopeptidase activity
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 401
ChainResidue
AHIS79
ATMG501
AHOH3071
AHOH3149
AHOH3196

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 402
ChainResidue
AHOH3158
AHOH3165
AASP97
AASP108
AGLU235
ACO403

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO A 403
ChainResidue
AASP108
AHIS171
ATHR202
AGLU204
AGLU235
ACO402
AHOH3158

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 404
ChainResidue
AGLU123
AHOH3093
AHOH3213
AHOH3222
AHOH3269

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 2001
ChainResidue
ASER72
AASN74
AVAL76
ASER231

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TMG A 501
ChainResidue
ACYS59
ATYR62
ATYR65
ACYS70
AHIS79
AHIS178
ATRP221
ACO401
AHOH3149

Functional Information from PROSITE/UniProt
site_idPS00680
Number of Residues19
DetailsMAP_1 Methionine aminopeptidase subfamily 1 signature. YcGHGIGqgfHeepqVl.HY
ChainResidueDetails
ATYR168-TYR186

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228
ChainResidueDetails
AHIS79
AHIS178

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729
ChainResidueDetails
AASP97
AASP108
AHIS171
AGLU204
AGLU235

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228
ChainResidueDetails
ATHR99

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU204
AGLN182

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU204

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PDB entries from 2024-07-17

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