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4L0D

Crystal structure of delta516-525 human cystathionine beta-synthase containing C-terminal 6xHis-tag

Functional Information from GO Data
ChainGOidnamespacecontents
A0001958biological_processendochondral ossification
A0001974biological_processblood vessel remodeling
A0004122molecular_functioncystathionine beta-synthase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006534biological_processcysteine metabolic process
A0006535biological_processcysteine biosynthetic process from serine
A0006563biological_processL-serine metabolic process
A0006565biological_processL-serine catabolic process
A0006801biological_processsuperoxide metabolic process
A0009069biological_processserine family amino acid metabolic process
A0010749biological_processregulation of nitric oxide mediated signal transduction
A0016829molecular_functionlyase activity
A0019343biological_processcysteine biosynthetic process via cystathionine
A0019344biological_processcysteine biosynthetic process
A0019346biological_processtranssulfuration
A0019448biological_processL-cysteine catabolic process
A0019825molecular_functionoxygen binding
A0019899molecular_functionenzyme binding
A0020037molecular_functionheme binding
A0021587biological_processcerebellum morphogenesis
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_processhomocysteine catabolic process
A0044272biological_processsulfur compound biosynthetic process
A0046872molecular_functionmetal ion binding
A0050421molecular_functionnitrite reductase (NO-forming) activity
A0050667biological_processhomocysteine metabolic process
A0051593biological_processresponse to folic acid
A0060135biological_processmaternal process involved in female pregnancy
A0060351biological_processcartilage development involved in endochondral bone morphogenesis
A0070025molecular_functioncarbon monoxide binding
A0070026molecular_functionnitric oxide binding
A0070814biological_processhydrogen sulfide biosynthetic process
A0071456biological_processcellular response to hypoxia
A0072341molecular_functionmodified amino acid binding
A0097746biological_processblood vessel diameter maintenance
A1904047molecular_functionS-adenosyl-L-methionine binding
B0001958biological_processendochondral ossification
B0001974biological_processblood vessel remodeling
B0004122molecular_functioncystathionine beta-synthase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006534biological_processcysteine metabolic process
B0006535biological_processcysteine biosynthetic process from serine
B0006563biological_processL-serine metabolic process
B0006565biological_processL-serine catabolic process
B0006801biological_processsuperoxide metabolic process
B0009069biological_processserine family amino acid metabolic process
B0010749biological_processregulation of nitric oxide mediated signal transduction
B0016829molecular_functionlyase activity
B0019343biological_processcysteine biosynthetic process via cystathionine
B0019344biological_processcysteine biosynthetic process
B0019346biological_processtranssulfuration
B0019448biological_processL-cysteine catabolic process
B0019825molecular_functionoxygen binding
B0019899molecular_functionenzyme binding
B0020037molecular_functionheme binding
B0021587biological_processcerebellum morphogenesis
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_processhomocysteine catabolic process
B0044272biological_processsulfur compound biosynthetic process
B0046872molecular_functionmetal ion binding
B0050421molecular_functionnitrite reductase (NO-forming) activity
B0050667biological_processhomocysteine metabolic process
B0051593biological_processresponse to folic acid
B0060135biological_processmaternal process involved in female pregnancy
B0060351biological_processcartilage development involved in endochondral bone morphogenesis
B0070025molecular_functioncarbon monoxide binding
B0070026molecular_functionnitric oxide binding
B0070814biological_processhydrogen sulfide biosynthetic process
B0071456biological_processcellular response to hypoxia
B0072341molecular_functionmodified amino acid binding
B0097746biological_processblood vessel diameter maintenance
B1904047molecular_functionS-adenosyl-L-methionine binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP A 601
ChainResidue
ALYS119
AGLY305
AILE306
ASER349
APRO375
AASP376
AASN149
ASER254
AVAL255
AGLY256
ATHR257
AGLY258
AGLY259
ATHR260

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HEM A 602
ChainResidue
AARG51
ACYS52
ATHR53
ATRP54
AGLU62
APRO64
AHIS65
AALA226
APRO229
AARG266

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP B 601
ChainResidue
BLYS119
BASN149
BVAL255
BGLY256
BTHR257
BGLY258
BTHR260
BGLY305
BILE306
BSER349
BPRO375
BASP376
BTYR381

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HEM B 602
ChainResidue
BARG51
BCYS52
BTHR53
BTRP54
BGLU62
BSER63
BPRO64
BHIS65
BALA226
BARG266
BVAL314

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 Residues4
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
ChainResidueDetails
ACYS52
AHIS65
BCYS52
BHIS65

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
ChainResidueDetails
BGLY256
BSER349
AASN149
AGLY256
ASER349
BASN149

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
BSER27
ASER27

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
ChainResidueDetails
ALYS119
BLYS119

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER199
ASER199

site_idSWS_FT_FI6
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:17087506
ChainResidueDetails
ALYS211
BLYS211

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 713
ChainResidueDetails
ALYS119covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay

site_idMCSA2
Number of Residues1
DetailsM-CSA 713
ChainResidueDetails
BLYS119covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay

221051

PDB entries from 2024-06-12

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