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5YR7

Human methionine aminopeptidase type 1b (F309L mutant)

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CO A 401
ChainResidue
AASP229
AASP240
AGLU367
ACO402
AMET406

site_idAC2
Number of Residues7
Detailsbinding site for residue CO A 402
ChainResidue
AGLU367
ACO401
AMET406
AASP240
AHIS303
ATHR334
AGLU336

site_idAC3
Number of Residues4
Detailsbinding site for residue CO A 403
ChainResidue
AHIS212
AMET406
AHOH545
AHOH561

site_idAC4
Number of Residues3
Detailsbinding site for residue CO A 404
ChainResidue
AHIS99
AHOH564
AHOH568

site_idAC5
Number of Residues5
Detailsbinding site for residue NA A 405
ChainResidue
AASN207
AVAL209
ASER363
AHOH544
AHOH560

site_idAC6
Number of Residues12
Detailsbinding site for residue MET A 406
ChainResidue
APHE198
AASP229
ATHR231
AASP240
AHIS303
AHIS310
AGLU336
ATRP353
AGLU367
ACO401
ACO402
ACO403

Functional Information from PROSITE/UniProt
site_idPS00680
Number of Residues19
DetailsMAP_1 Methionine aminopeptidase subfamily 1 signature. YcGHGIHkllHtapnVp.HY
ChainResidueDetails
ATYR300-TYR318

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291
ChainResidueDetails
AHIS212
AHIS310

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291
ChainResidueDetails
AASP229
AASP240
AHIS303
AGLU336
AGLU367

224572

PDB entries from 2024-09-04

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