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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4L27

Crystal structure of delta1-39 and delta516-525 human cystathionine beta-synthase D444N mutant containing C-terminal 6xHis tag

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_processcysteine biosynthetic process from serine
A0006563biological_processL-serine metabolic process
A0006565biological_processL-serine catabolic process
A0008652biological_processamino acid biosynthetic process
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
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
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_processcysteine biosynthetic process from serine
B0006563biological_processL-serine metabolic process
B0006565biological_processL-serine catabolic process
B0008652biological_processamino acid biosynthetic process
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
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
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
C0003824molecular_functioncatalytic activity
C0004122molecular_functioncystathionine beta-synthase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006534biological_processcysteine metabolic process
C0006535biological_processcysteine biosynthetic process from serine
C0006563biological_processL-serine metabolic process
C0006565biological_processL-serine catabolic process
C0008652biological_processamino acid biosynthetic process
C0016829molecular_functionlyase activity
C0019343biological_processcysteine biosynthetic process via cystathionine
C0019344biological_processcysteine biosynthetic process
C0019346biological_processtranssulfuration
C0019448biological_processL-cysteine catabolic process
C0019825molecular_functionoxygen binding
C0019899molecular_functionenzyme binding
C0020037molecular_functionheme binding
C0030170molecular_functionpyridoxal phosphate binding
C0031625molecular_functionubiquitin protein ligase binding
C0031667biological_processresponse to nutrient levels
C0042262biological_processDNA protection
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0043066biological_processnegative regulation of apoptotic process
C0043418biological_processhomocysteine catabolic process
C0044272biological_processsulfur compound biosynthetic process
C0046872molecular_functionmetal ion binding
C0050421molecular_functionnitrite reductase (NO-forming) activity
C0050667biological_processhomocysteine metabolic process
C0070025molecular_functioncarbon monoxide binding
C0070026molecular_functionnitric oxide binding
C0070814biological_processhydrogen sulfide biosynthetic process
C0071456biological_processcellular response to hypoxia
C0072341molecular_functionmodified amino acid binding
C1904047molecular_functionS-adenosyl-L-methionine binding
D0003824molecular_functioncatalytic activity
D0004122molecular_functioncystathionine beta-synthase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006534biological_processcysteine metabolic process
D0006535biological_processcysteine biosynthetic process from serine
D0006563biological_processL-serine metabolic process
D0006565biological_processL-serine catabolic process
D0008652biological_processamino acid biosynthetic process
D0016829molecular_functionlyase activity
D0019343biological_processcysteine biosynthetic process via cystathionine
D0019344biological_processcysteine biosynthetic process
D0019346biological_processtranssulfuration
D0019448biological_processL-cysteine catabolic process
D0019825molecular_functionoxygen binding
D0019899molecular_functionenzyme binding
D0020037molecular_functionheme binding
D0030170molecular_functionpyridoxal phosphate binding
D0031625molecular_functionubiquitin protein ligase binding
D0031667biological_processresponse to nutrient levels
D0042262biological_processDNA protection
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0043066biological_processnegative regulation of apoptotic process
D0043418biological_processhomocysteine catabolic process
D0044272biological_processsulfur compound biosynthetic process
D0046872molecular_functionmetal ion binding
D0050421molecular_functionnitrite reductase (NO-forming) activity
D0050667biological_processhomocysteine metabolic process
D0070025molecular_functioncarbon monoxide binding
D0070026molecular_functionnitric oxide binding
D0070814biological_processhydrogen sulfide biosynthetic process
D0071456biological_processcellular response to hypoxia
D0072341molecular_functionmodified amino acid binding
D1904047molecular_functionS-adenosyl-L-methionine binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP B 601
ChainResidue
BLYS119
BILE306
BSER349
BPRO375
BASP376
BTYR381
BSER147
BASN149
BVAL255
BGLY256
BTHR257
BGLY258
BGLY259
BTHR260
site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM B 602
ChainResidue
BARG51
BCYS52
BTHR53
BTRP54
BARG58
BGLU62
BSER63
BPRO64
BHIS65
BARG224
BALA226
BPRO229
BLEU230
BTYR233
BARG266
BVAL314
site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP D 601
ChainResidue
DLYS119
DASN149
DSER254
DVAL255
DGLY256
DTHR257
DGLY258
DGLY259
DTHR260
DGLY305
DILE306
DSER349
DPRO375
DASP376
DTYR381
site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM D 602
ChainResidue
DPRO49
DSER50
DARG51
DCYS52
DTHR53
DTRP54
DARG58
DPRO59
DGLU62
DSER63
DPRO64
DHIS65
DARG224
DALA226
DPRO229
DTYR233
DARG266
DTHR313
site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 601
ChainResidue
ALYS119
AASN149
ASER254
AVAL255
AGLY256
ATHR257
AGLY258
AGLY259
ATHR260
AGLU304
AILE306
ASER349
APRO375
AASP376
ATYR381
site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 602
ChainResidue
ASER50
AARG51
ACYS52
ATHR53
ATRP54
AARG58
ASER63
APRO64
AHIS65
AALA226
APRO229
ATHR262
AGLY263
AARG266
ATHR313
AVAL314
DARG51
site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP C 601
ChainResidue
CTHR257
CGLY258
CGLY259
CTHR260
CILE306
CSER349
CPRO375
CASP376
CTYR381
CLYS119
CASN149
CVAL255
CGLY256
site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM C 602
ChainResidue
CPRO49
CSER50
CARG51
CCYS52
CTHR53
CTRP54
CSER63
CPRO64
CHIS65
CARG224
CALA226
CPRO229
CTYR233
CGLY263
CARG266
CVAL314
Functional Information from PROSITE/UniProt
site_idPS00901
Number of Residues19
DetailsCYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KcEffn.AGgSVKdRiSlrM
ChainResidueDetails
BLYS108-MET126
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
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_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11483494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12173932","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
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_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"17087506","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues58
DetailsDomain: {"description":"CBS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
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
site_idMCSA3
Number of Residues1
DetailsM-CSA 713
ChainResidueDetails
CLYS119covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay
site_idMCSA4
Number of Residues1
DetailsM-CSA 713
ChainResidueDetails
DLYS119covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay

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PDB entries from 2025-12-17

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