Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1m54a_ Alpha and beta proteins (a/b) Tryptophan synthase beta subunit-like PLP-dependent enzymes Tryptophan synthase beta subunit-like PLP-dependent enzymes Tryptophan synthase beta subunit-like PLP-dependent enzymes Cystathionine beta-synthase human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Bd1m54b_ Alpha and beta proteins (a/b) Tryptophan synthase beta subunit-like PLP-dependent enzymes Tryptophan synthase beta subunit-like PLP-dependent enzymes Tryptophan synthase beta subunit-like PLP-dependent enzymes Cystathionine beta-synthase human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Cd1m54c_ Alpha and beta proteins (a/b) Tryptophan synthase beta subunit-like PLP-dependent enzymes Tryptophan synthase beta subunit-like PLP-dependent enzymes Tryptophan synthase beta subunit-like PLP-dependent enzymes Cystathionine beta-synthase human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Dd1m54d_ Alpha and beta proteins (a/b) Tryptophan synthase beta subunit-like PLP-dependent enzymes Tryptophan synthase beta subunit-like PLP-dependent enzymes Tryptophan synthase beta subunit-like PLP-dependent enzymes Cystathionine beta-synthase human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ed1m54e_ Alpha and beta proteins (a/b) Tryptophan synthase beta subunit-like PLP-dependent enzymes Tryptophan synthase beta subunit-like PLP-dependent enzymes Tryptophan synthase beta subunit-like PLP-dependent enzymes Cystathionine beta-synthase human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Fd1m54f_ Alpha and beta proteins (a/b) Tryptophan synthase beta subunit-like PLP-dependent enzymes Tryptophan synthase beta subunit-like PLP-dependent enzymes Tryptophan synthase beta subunit-like PLP-dependent enzymes Cystathionine beta-synthase human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyTryptophan synthase beta subunit-like PLP-dependent enzymes 8034316 3001427 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyTryptophan synthase beta subunit-like PLP-dependent enzymes 8034316 3001427 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyTryptophan synthase beta subunit-like PLP-dependent enzymes 8034316 3001427 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyTryptophan synthase beta subunit-like PLP-dependent enzymes 8034316 3001427 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyTryptophan synthase beta subunit-like PLP-dependent enzymes 8034316 3001427 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyTryptophan synthase beta subunit-like PLP-dependent enzymes 8034316 3001427 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APALPe1m54A1 A: a/b three-layered sandwichesX: Rossmann-likeH: Tryptophan synthase beta subunit-like PLP-dependent enzymes (From Topology)T: Tryptophan synthase beta subunit-like PLP-dependent enzymesF: PALPECOD (1.6)
BPALPe1m54B1 A: a/b three-layered sandwichesX: Rossmann-likeH: Tryptophan synthase beta subunit-like PLP-dependent enzymes (From Topology)T: Tryptophan synthase beta subunit-like PLP-dependent enzymesF: PALPECOD (1.6)
CPALPe1m54C1 A: a/b three-layered sandwichesX: Rossmann-likeH: Tryptophan synthase beta subunit-like PLP-dependent enzymes (From Topology)T: Tryptophan synthase beta subunit-like PLP-dependent enzymesF: PALPECOD (1.6)
DPALPe1m54D2 A: a/b three-layered sandwichesX: Rossmann-likeH: Tryptophan synthase beta subunit-like PLP-dependent enzymes (From Topology)T: Tryptophan synthase beta subunit-like PLP-dependent enzymesF: PALPECOD (1.6)
EPALPe1m54E1 A: a/b three-layered sandwichesX: Rossmann-likeH: Tryptophan synthase beta subunit-like PLP-dependent enzymes (From Topology)T: Tryptophan synthase beta subunit-like PLP-dependent enzymesF: PALPECOD (1.6)
FPALPe1m54F1 A: a/b three-layered sandwichesX: Rossmann-likeH: Tryptophan synthase beta subunit-like PLP-dependent enzymes (From Topology)T: Tryptophan synthase beta subunit-like PLP-dependent enzymesF: PALPECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.40.50.1100 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold CATH (4.3.0)
B3.40.50.1100 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold CATH (4.3.0)
C3.40.50.1100 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold CATH (4.3.0)
D3.40.50.1100 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold CATH (4.3.0)
E3.40.50.1100 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold CATH (4.3.0)
F3.40.50.1100 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D, E
PF00291Pyridoxal-phosphate dependent enzyme (PALP)Pyridoxal-phosphate dependent enzyme- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D, E
CYSTATHIONINE BETA-SYNTHASE

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
cystathionine beta-synthase  M-CSA #713

Mammalian cystathionine beta-synthase (CBS) is a heme protein that catalyses the conversion of L-serine and L-homocysteine (L-Hcys) to give cystathionine in the first step in the transulfuration pathway. CBS is a member of the beta-family (Fold-type II) of pyridoxal 5'-phosphate (PLP) enzymes. These catalyse PLP-dependent, beta-replacement reactions in which the electronegative substituent in the beta-position of the amino acid substrate (in the case of CBS, the -OH group of L-Ser), is replaced by a sulphur-containing nucleophile (L-Hcys thiol group). Human CBS (hCBS) has three domains - the N-terminal domain where heme, which is not essential for catalysis and the function of which is still uncertain, is bound; the core catalytic dimeric domain where PLP is bound; and the C-terminal domain where the allosteric activator of the enzyme, S-adenosyl-L-methionine (AdoMet), is bound.

Defined by 1 residue: LYS:A-76 [auth A-119]
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EC: 4.2.1.22 (PDB Primary Data)