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6Z4N

CRYSTAL STRUCTURE OF OASS COMPLEXED WITH UPAR INHIBITOR

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0004124molecular_functioncysteine synthase activity
AAA0005737cellular_componentcytoplasm
AAA0006535biological_processcysteine biosynthetic process from serine
AAA0016740molecular_functiontransferase activity
AAA0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
AAA0019344biological_processcysteine biosynthetic process
AAA0080146molecular_functionL-cysteine desulfhydrase activity
BBB0004124molecular_functioncysteine synthase activity
BBB0005737cellular_componentcytoplasm
BBB0006535biological_processcysteine biosynthetic process from serine
BBB0016740molecular_functiontransferase activity
BBB0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
BBB0019344biological_processcysteine biosynthetic process
BBB0080146molecular_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. KvEsrn.PSfSVKcRiGanM
ChainResidueDetails
AAALYS30-MET48

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:11023792
ChainResidueDetails
BBBASN7
AAAASN7

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: in other chain => ECO:0000305|PubMed:11023792
ChainResidueDetails
BBBARG34
BBBLEU268
AAALEU268
AAAARG34

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10452898, ECO:0000269|PubMed:11023792, ECO:0000269|PubMed:9761678
ChainResidueDetails
BBBASN71
BBBSER272
AAAASN71
AAASER272

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING:
ChainResidueDetails
BBBGLY176
AAAGLY176

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
BBBLYS41
AAALYS41

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 865
ChainResidueDetails
AAALYS41covalent catalysis, proton shuttle (general acid/base)
AAASER272electrostatic stabiliser

site_idMCSA2
Number of Residues2
DetailsM-CSA 865
ChainResidueDetails
BBBLYS41covalent catalysis, proton shuttle (general acid/base)
BBBSER272electrostatic stabiliser

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PDB entries from 2024-05-15

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