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Ligands
Code Name Style Show Link
MET Methionine
PLP Pyridoxal-5'-phosphate
Non-standard Residues
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Glycosylation
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Code : 1D6S   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : CRYSTAL STRUCTURE OF THE K41A MUTANT OF O-ACETYLSERINE SULFHYDRYLASE COMPLEXED IN EXTERNAL ALDIMINE LINKAGE WITH METHIONINE
Release Data : 2000-04-15
Compound :
mol_id molecule chains
1 O-ACETYLSERINE SULFHYDRYLASE A,B
ec: 4.2.99.8
mutation: K41A
Source :
mol_id organism_scientific expression_system
1 Salmonella typhimurium  (taxid:602) Escherichia coli  (taxid:562)
strain: DW378
Authors : Burkhard, P., Tai, C.H., Ristroph, C.M., Cook, P.F., Jansonius, J.N.
Keywords : CYSTEINE BIOSYNTHESIS, BETA REPLACEMENT ENZYME, PLP, K41A, LYASE
Exp. method : X-RAY DIFFRACTION ( 2.30 Å )
Citation :

Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium.

Burkhard, P.,Tai, C.H.,Ristroph, C.M.  et al.
(1999)  J.Mol.Biol.  291 : 941 - 953

PubMed: 10452898
DOI: 10.1006/jmbi.1999.3002

Three-dimensional Structure of O-Acetylserine Sulfhydrylase from Salmonella typhimurium

Burkhard, P.,Rao, G.S.,Hohenester, E.  et al.
(1998)  J.Mol.Biol.  283 : 121 - 133

DOI: 10.1006/jmbi.1998.2037

Chain : A, B
UniProt : P12674 (CYSK_SALTY)
Reaction: EC: Evidence:
Physiological Direction:
hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine 2.5.1.47 PubMed:4977445
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