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Crystal Structure of Modified Serine Racemase complexed with Serine

Source organism: Schizosaccharomyces pombe
Biochemical function: metal ion binding
Biological process: D-serine metabolic process
Cellular component: cellular_component

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EC 4.3.1.18: D-serine ammonia-lyase

Reaction catalysed:
(1a) D-serine = 2-aminoprop-2-enoate + H(2)O
Systematic name:
D-serine ammonia-lyase (pyruvate-forming)
Alternative Name(s):
  • D-hydroxy amino acid dehydratase
  • D-hydroxyaminoacid dehydratase
  • D-serine deaminase
  • D-serine dehydrase
  • D-serine dehydratase
  • D-serine dehydratase (deaminating)
  • D-serine hydro-lyase (deaminating)
  • D-serine hydrolase

EC 4.3.1.17: L-serine ammonia-lyase

Reaction catalysed:
(1a) L-serine = 2-aminoprop-2-enoate + H(2)O
Systematic name:
L-serine ammonia-lyase (pyruvate-forming)
Alternative Name(s):
  • L-hydroxyaminoacid dehydratase
  • L-serine deaminase
  • L-serine dehydratase
  • L-serine hydro-lyase (deaminating)
  • Serine deaminase

EC 5.1.1.18: Serine racemase

Reaction catalysed:
L-serine = D-serine
Systematic name:
Serine racemase
Alternative Name(s):
  • SRR

GO terms

Sequence family

Pfam Protein family (Pfam)
PF00291
Domain description: Pyridoxal-phosphate dependent enzyme
Occurring in:
  1. Serine racemase
The deposited structure of PDB entry 2zr8 contains 1 copy of Pfam domain PF00291 (Pyridoxal-phosphate dependent enzyme) in Serine racemase. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR036052
Domain description: Tryptophan synthase beta chain-like, PALP domain superfamily
Occurring in:
  1. Serine racemase
IPR001926
Domain description: Tryptophan synthase beta chain-like, PALP domain
Occurring in:
  1. Serine racemase

Structure domain

CATH CATH domain
3.40.50.1100
Class: Alpha Beta
Architecture: 3-Layer(aba) Sandwich
Topology: Rossmann fold
Homology: Rossmann fold
Occurring in:
  1. Serine racemase
The deposited structure of PDB entry 2zr8 contains 2 copies of CATH domain 3.40.50.1100 (Rossmann fold) in Serine racemase. Showing 2 copies in chain A.

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