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5YKP

Human methionine aminopeptidase type 1b (F309M mutant) in complex with ovalicin

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue CO A 401
ChainResidue
AASP240
AHIS303
ATHR334
AGLU336
AGLU367
ACO402
AOVA405
AHOH521

site_idAC2
Number of Residues6
Detailsbinding site for residue CO A 402
ChainResidue
AASP240
AGLU367
ACO401
AHOH521
AHOH594
AASP229

site_idAC3
Number of Residues4
Detailsbinding site for residue CO A 403
ChainResidue
AGLU128
ATYR195
AHIS310
AHOH597

site_idAC4
Number of Residues5
Detailsbinding site for residue K A 404
ChainResidue
ASER205
AASN207
AVAL209
ASER363
AHOH683

site_idAC5
Number of Residues9
Detailsbinding site for residue OVA A 405
ChainResidue
ATYR195
AHIS212
ATYR300
ACYS301
AGLU336
ACO401
AHOH521
AHOH601
AHOH670

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03174","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16724298","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16823043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17114291","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03174","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16274222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16724298","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16823043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17114291","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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