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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: BINDING => ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291
ChainResidueDetails
AHIS310
AHIS212

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
AGLU336
AGLU367
AASP229
AASP240
AHIS303

218500

PDB entries from 2024-04-17

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