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Structure paper

TitlePyridomycin bridges the NADH- and substrate-binding pockets of the enoyl reductase InhA.
Journal, issue, pagesNat. Chem. Biol., Vol. 10, Page 96-98, Year 2014
Publish dateMar 26, 2013 (structure data deposition date)
AuthorsHartkoorn, R.C. / Pojer, F. / Read, J.A. / Gingell, H. / Neres, J. / Horlacher, O.P. / Altmann, K.H. / Cole, S.T.
External linksNat. Chem. Biol. / PubMed:24292073
MethodsX-ray diffraction
Resolution1.95 - 2.25 Å
Structure data

PDB-4bge:
Crystal structure of InhA(S94A) mutant in complex with pyridomycin
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-4bgi:
Crystal structure of InhA(S94A) mutant in complex with OH-141
Method: X-RAY DIFFRACTION / Resolution: 2.09 Å

PDB-4bii:
How nature bridges the gap: Crystallographic elucidation of pyridomycin binding to InhA
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-PYW:
Pyridomycin

ChemComp-HOH:
WATER

ChemComp-I4I:
3-hydroxy-N-[(2R,5R,6S,9S,10S,11R)-10-hydroxy-5,11-dimethyl-3,7,12-trioxo-2-(propan-2-yl)-9-(pyridin-3-ylmethyl)-1,4-dioxa-8-azacyclododecan-6-yl]pyridine-2-carboxamide

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

Source
  • mycobacterium tuberculosis (strain atcc 25618 / h37rv) (bacteria)
  • mycobacterium tuberculosis (bacteria)
KeywordsOXIDOREDUCTASE / TUBERCULOSIS DRUG / ACP ENOYL REDUCTASE

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