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7YOF

Crystal Structure of Triple mutant (D67E, A68P, I88L) of O-acetyl-L-serine sulfhydrylase from Haemophilus influenzae at 2.3 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004124molecular_functioncysteine synthase activity
A0005737cellular_componentcytoplasm
A0006535biological_processcysteine biosynthetic process from serine
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0019344biological_processcysteine biosynthetic process
A0080146molecular_functionL-cysteine desulfhydrase activity
Functional Information from PROSITE/UniProt
site_idPS00901
Number of Residues19
DetailsCYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KiEgrn.PSySVKcRiGanM
ChainResidueDetails
ALYS31-MET49

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A1E3
ChainResidueDetails
AASN7

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P0A1E3
ChainResidueDetails
AARG35
ALEU268

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN72
AGLY177
ASER272

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALLP42

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PDB entries from 2024-11-06

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