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5YR5

Human methionine aminopeptidase type 1b (F309L 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
AHOH455

site_idAC2
Number of Residues6
Detailsbinding site for residue CO A 402
ChainResidue
AASP240
AGLU367
ACO401
AHOH447
AHOH455
AASP229

site_idAC3
Number of Residues6
Detailsbinding site for residue CO A 403
ChainResidue
AGLU128
ATYR195
ATYR196
AHIS310
AHOH612
AHOH613

site_idAC4
Number of Residues4
Detailsbinding site for residue NA A 404
ChainResidue
AASN207
AVAL209
ASER363
AHOH440

site_idAC5
Number of Residues11
Detailsbinding site for residue OVA A 405
ChainResidue
ATYR195
AHIS212
ATYR300
ACYS301
AHIS303
AGLU336
ACO401
AHOH438
AHOH455
AHOH580
AHOH585

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

218853

PDB entries from 2024-04-24

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