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

1D6S

CRYSTAL STRUCTURE OF THE K41A MUTANT OF O-ACETYLSERINE SULFHYDRYLASE COMPLEXED IN EXTERNAL ALDIMINE LINKAGE WITH METHIONINE

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
B0004124molecular_functioncysteine synthase activity
B0005737cellular_componentcytoplasm
B0006535biological_processcysteine biosynthetic process from serine
B0016740molecular_functiontransferase activity
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0019344biological_processcysteine biosynthetic process
B0080146molecular_functionL-cysteine desulfhydrase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MET A 401
ChainResidue
ATHR68
AASN69
AGLY70
AASN71
ATHR72
AGLN142
AGLY228
APLP501

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP A 501
ChainResidue
AASN71
AGLY176
ATHR177
AGLY178
AGLY179
ATHR180
AGLY228
AILE229
ASER272
APRO299
ASER300
ATYR305
AMET401
AHOH508
AHOH579
AASN69

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PLP B 502
ChainResidue
BASN69
BASN71
BGLY174
BGLY176
BTHR177
BGLY178
BTHR180
BGLN227
BGLY228
BILE229
BSER272
BPRO299
BSER300
BTYR305
BMET402
BHOH509
BHOH514
BHOH565

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MET B 402
ChainResidue
BTHR68
BASN69
BGLY70
BASN71
BTHR72
BMET119
BGLN142
BGLY228
BPLP502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:11023792
ChainResidueDetails
ASER8
BSER8

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: in other chain => ECO:0000305|PubMed:11023792
ChainResidueDetails
AASN35
AALA269
BASN35
BALA269

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10452898, ECO:0000269|PubMed:11023792, ECO:0000269|PubMed:9761678
ChainResidueDetails
ATHR72
ASER273
BTHR72
BSER273

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ATHR177
BTHR177

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ACYS42
BCYS42

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1oas
ChainResidueDetails
ASER272
AALA41

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1oas
ChainResidueDetails
BSER272
BALA41

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oas
ChainResidueDetails
AALA41

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oas
ChainResidueDetails
BALA41

site_idMCSA1
Number of Residues2
DetailsM-CSA 865
ChainResidueDetails
ACYS42covalent catalysis, proton shuttle (general acid/base)
ASER273electrostatic stabiliser

site_idMCSA2
Number of Residues2
DetailsM-CSA 865
ChainResidueDetails
BCYS42covalent catalysis, proton shuttle (general acid/base)
BSER273electrostatic stabiliser

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon