Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4U73

HsMetAP(F309M) IN COMPLEX WITH (amino(phenyl)methyl)phosphonic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CO A 401
ChainResidue
AASP240
AHIS303
AGLU336
AGLU367
ACO402
AQ02404

site_idAC2
Number of Residues5
Detailsbinding site for residue CO A 402
ChainResidue
ACO401
AQ02404
AASP229
AASP240
AGLU367

site_idAC3
Number of Residues4
Detailsbinding site for residue K A 403
ChainResidue
AASN207
AVAL209
ASER363
AHOH736

site_idAC4
Number of Residues13
Detailsbinding site for residue Q02 A 404
ChainResidue
ATYR195
AHIS212
AASP229
ATHR231
AASP240
AHIS303
AHIS310
AGLU336
AGLU367
ACO401
ACO402
AHOH720
AHOH733

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: 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

PDB statisticsPDBj update infoContact PDBjnumon