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5YR6

Human methionine aminopeptidase type 1b (F309L mutant) in complex with TNP470

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
ATN4410
AHOH469

site_idAC2
Number of Residues6
Detailsbinding site for residue CO A 402
ChainResidue
AASP240
AGLU367
ACO401
AHOH451
AHOH469
AASP229

site_idAC3
Number of Residues4
Detailsbinding site for residue NA A 403
ChainResidue
AASN207
AVAL209
ASER363
AHOH441

site_idAC4
Number of Residues13
Detailsbinding site for residue TN4 A 410
ChainResidue
APRO192
ATYR195
AHIS212
ATYR300
ACYS301
AHIS310
AGLU336
ATRP353
ACO401
AHOH444
AHOH469
AHOH544
AHOH574

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 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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