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2Q93

E. coli methionine aminopeptidase Mn-form with inhibitor B21

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 Residues6
DetailsBINDING SITE FOR RESIDUE MN A 301
ChainResidue
AASP108
AHIS171
AGLU204
AGLU235
AMN302
AB21400

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 302
ChainResidue
AMN301
AB21400
AHOH505
AASP97
AASP108
AGLU235

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 500
ChainResidue
AASN74
AVAL76
ASER231
AHOH517

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE B21 A 400
ChainResidue
ATYR62
ATYR65
AHIS79
AASP97
AASP108
AHIS171
AHIS178
AGLU204
ATRP221
AGLU235
AMN301
AMN302
AHOH505

Functional Information from PROSITE/UniProt
site_idPS00680
Number of Residues19
DetailsMAP_1 Methionine aminopeptidase subfamily 1 signature. YcGHGIGrgfHeepqVl.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

227561

PDB entries from 2024-11-20

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