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EBI PDBe PDBeView

PDBe Entry: 1ogz view

CRYSTAL STRUCTURE OF 5-3-KETOSTEROID ISOMERASE MUTANTS P39A COMPLEXED WITH EQUILENIN FROM PSEUDOMONAS TESTOSTERONI
Summary
Header ISOMERASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.3 Å, R-factor: 23.5%, Free R-factor: 30.9%, Spacegroup: P 65 2 2
Released 04/09/2003, deposition: 20/05/2003, last revision: 24/02/2009
Authors Nam, G.H.search; Cha, S.-S.search; Yun, Y.S.search; Oh, Y.H.search; Hong, B.H.search; Lee, H.-S.search; Choi, K.Y.search
Primary citation The Conserved Cis-Pro39 Residue Plays a Crucial Role in the Proper Positioning of the Catalytic Base Asp38 in Ketosteroid Isomerase from Comamonas Testosteroni.
BIOCHEM.J.search vol:375, pag:297 (2003) [PubMed ID 12852789 ]search
Keywords KETOSTEROIDsearch, ISOMERASEsearch
EC 5.3.3.1 ExPASy BRENDA search (A)
Organism Comamonas testosteroni 285search(A)
UniProt Steroid Delta-isomerase (EC 5.3.3.1) (Delta(5)-3-ketosteroid isomerase) P00947search (A)
Solvent A
Related entries 1buq, 1isk, 1ocv, 1ohp, 1ohs, 1qjg, 8cho
Polymers
Id Name Type UniProt Residues Observed
A STEROID DELTA-ISOMERASE Protein P00947 (SDIS_COMTE)search
 125 100%
Heterogens
Id Name Ligands
A EQUILENIN EQU search
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