Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9HIF

Crystal Structure of Human cystathionine beta-synthase variant R336C

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004122molecular_functioncystathionine beta-synthase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006534biological_processcysteine metabolic process
A0006535biological_processL-cysteine biosynthetic process from L-serine
A0006563biological_processL-serine metabolic process
A0006565biological_processL-serine catabolic process
A0008652biological_processamino acid biosynthetic process
A0016829molecular_functionlyase activity
A0019343biological_processL-cysteine biosynthetic process via L-cystathionine
A0019344biological_processL-cysteine biosynthetic process
A0019346biological_processtranssulfuration
A0019448biological_processL-cysteine catabolic process
A0019825molecular_functionoxygen binding
A0019899molecular_functionenzyme binding
A0020037molecular_functionheme binding
A0030170molecular_functionpyridoxal phosphate binding
A0031625molecular_functionubiquitin protein ligase binding
A0031667biological_processresponse to nutrient levels
A0042262biological_processDNA protection
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043066biological_processnegative regulation of apoptotic process
A0043418biological_processL-homocysteine catabolic process
A0044272biological_processsulfur compound biosynthetic process
A0046872molecular_functionmetal ion binding
A0050421molecular_functionnitrite reductase (NO-forming) activity
A0050667biological_processhomocysteine metabolic process
A0070025molecular_functioncarbon monoxide binding
A0070026molecular_functionnitric oxide binding
A0070814biological_processhydrogen sulfide biosynthetic process
A0071456biological_processcellular response to hypoxia
A0072341molecular_functionmodified amino acid binding
A1904047molecular_functionS-adenosyl-L-methionine binding
B0003824molecular_functioncatalytic activity
B0004122molecular_functioncystathionine beta-synthase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006534biological_processcysteine metabolic process
B0006535biological_processL-cysteine biosynthetic process from L-serine
B0006563biological_processL-serine metabolic process
B0006565biological_processL-serine catabolic process
B0008652biological_processamino acid biosynthetic process
B0016829molecular_functionlyase activity
B0019343biological_processL-cysteine biosynthetic process via L-cystathionine
B0019344biological_processL-cysteine biosynthetic process
B0019346biological_processtranssulfuration
B0019448biological_processL-cysteine catabolic process
B0019825molecular_functionoxygen binding
B0019899molecular_functionenzyme binding
B0020037molecular_functionheme binding
B0030170molecular_functionpyridoxal phosphate binding
B0031625molecular_functionubiquitin protein ligase binding
B0031667biological_processresponse to nutrient levels
B0042262biological_processDNA protection
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043066biological_processnegative regulation of apoptotic process
B0043418biological_processL-homocysteine catabolic process
B0044272biological_processsulfur compound biosynthetic process
B0046872molecular_functionmetal ion binding
B0050421molecular_functionnitrite reductase (NO-forming) activity
B0050667biological_processhomocysteine metabolic process
B0070025molecular_functioncarbon monoxide binding
B0070026molecular_functionnitric oxide binding
B0070814biological_processhydrogen sulfide biosynthetic process
B0071456biological_processcellular response to hypoxia
B0072341molecular_functionmodified amino acid binding
B1904047molecular_functionS-adenosyl-L-methionine binding
Functional Information from PROSITE/UniProt
site_idPS00901
Number of Residues19
DetailsCYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KcEffn.AGgSVKdRiSlrM
ChainResidueDetails
ALYS108-MET126

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues116
DetailsDomain: {"description":"CBS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11483494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12173932","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11483494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12173932","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"11483494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12173932","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"17087506","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 713
ChainResidueDetails
ALLP119covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay

site_idMCSA2
Number of Residues1
DetailsM-CSA 713
ChainResidueDetails
BLLP119covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay

249697

PDB entries from 2026-02-25

PDB statisticsPDBj update infoContact PDBjnumon