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4ZU6

Crystal Structure of O-Acetylserine Sulfhydrylase from Haemophilus influenzae in complex with pre-reactive o-acetyl serine, alpha-aminoacrylate reaction intermediate and Peptide inhibitor at the resolution of 2.25A

Replaces:  4MH9
Functional Information from GO Data
ChainGOidnamespacecontents
X0004124molecular_functioncysteine synthase activity
X0005737cellular_componentcytoplasm
X0006535biological_processcysteine biosynthetic process from serine
X0016740molecular_functiontransferase activity
X0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
X0019344biological_processcysteine biosynthetic process
X0080146molecular_functionL-cysteine desulfhydrase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue OAS X 401
ChainResidue
XTHR69
XHOH537
XSER70
XASN72
XTHR73
XGLN143
XPHE144
XGLY177
XGLY228
XPLP402

site_idAC2
Number of Residues21
Detailsbinding site for residue PLP X 402
ChainResidue
XLYS42
XASN72
XGLY175
XVAL176
XGLY177
XTHR178
XGLY179
XGLY180
XSER181
XGLN227
XGLY228
XILE229
XSER272
XPRO299
XSER300
XTYR305
XOAS401
XHOH513
XHOH531
XHOH535
XHOH556

Functional Information from PROSITE/UniProt
site_idPS00901
Number of Residues19
DetailsCYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KiEgrn.PSySVKcRiGanM
ChainResidueDetails
XLYS31-MET49

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A1E3
ChainResidueDetails
XASN7

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P0A1E3
ChainResidueDetails
XARG35
XLEU268

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
XASN72
XGLY177
XSER272

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
XLYS42

223166

PDB entries from 2024-07-31

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