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EBI PDBe PDBeView

PDBe Entry: 2nmp view

Crystal structure of human Cystathionine gamma lyase
Summary
Header LYASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.6 Å, R-factor: 18.035%, Free R-factor: 24.454%, Spacegroup: P 21 21 21
Released 07/11/2006, deposition: 23/10/2006, last revision: 31/03/2009
Authors Karlberg, T.search; Uppenberg, J.search; Arrowsmith, C.search; Berglund, H.search; Busam, R.D.search; Collins, R.search; Edwards, A.search; Ericsson, U.B.search; Flodin, S.search; Flores, A.search; Graslund, S.search; Hallberg, B.M.search; Hammarstrom, M.search; Hogbom, M.search; Johansson, I.search; Kotenyova, T.search; Magnusdottir, A.search; Moche, M.search; Nilsson, M.E.search; Nordlund, P.search; Nyman, T.search; Ogg, D.search; Persson, C.search; Sagemark, J.search; Stenmark, P.search; Sundstrom, M.search; Thorsell, A.G.search; van-den-Berg, S.search; Wallden, K.search; Weigelt, J.search; Holmberg-Schiavone, L.search; Structural Genomics Consortium (SGC)search
Primary citation Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S
J.BIOL.CHEM.search vol:284, pag:3076-3085 (2009) [PubMed ID 19019829 ]search
Keywords amino-acid biosynthesissearch, lyasesearch, pyridoxal phopshatesearch, structural genomicssearch, Structural Genomics Consortiumsearch, SGCsearch
EC 4.4.1.1 ExPASy BRENDA search (A B C D)
Organism Homo sapiens(human) 9606search(A B C D)
UniProt Cystathionine gamma-lyase (EC 4.4.1.1) (Gamma-cystathionase) P32929search (A B C D)
Solvent A, B, C, D
Polymers
Id Name Type UniProt Residues Observed
A, B, C, D Cystathionine gamma-lyase Protein P32929 (CGL_HUMAN)search
 403 96%
Heterogens
Id Name Ligands
A, C, D PYRIDOXAL-5'-PHOSPHATE PLP search
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