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4LI3

Crystal Structure of O-Acetylserine Sulfhydrylase from Haemophilus influenzae in complex with high affinity inhibitory peptide from Serine acetyl transferase of Salmonella typhimurium

Functional Information from GO Data
ChainGOidnamespacecontents
X0003824molecular_functioncatalytic activity
X0004124molecular_functioncysteine synthase activity
X0005737cellular_componentcytoplasm
X0006535biological_processcysteine biosynthetic process from serine
X0008652biological_processamino acid biosynthetic process
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 Residues5
DetailsBINDING SITE FOR RESIDUE GOL X 401
ChainResidue
XVAL249
XASP250
XALA278
XARG282
XHOH522

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 site: {"evidences":[{"source":"UniProtKB","id":"P0A1E3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0A1E3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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