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Article

Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state.

Journal of molecular biology - 5 Mar 1992

Müller C W, Schulz G E

Abstract excerpt

The structure of adenylate kinase from Escherichia coli ligated with the two-substrate-mimicking inhibitor P1,P5-bis(adenosine-5'-)pentaphosphate has been determined by X-ray diffraction and refined to a resolution of 1.9 A. The asymmetric unit of the crystals contains two copies of the complex, the structures of which agree well with each other. One of these copies is less well ordered in the crystals than the...

Topics

Adenosine Monophosphate
Adenosine Triphosphate
Adenylate Kinase
Amino Acid Sequence
Binding Sites
Dinucleoside Phosphates
Escherichia coli
Hydrogen Bonding
Models, Molecular
Molecular Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Substrate Specificity

X-Ray Diffraction

Source

Identifiers

PMID: 1548697
DOI: 10.1016/0022-2836(92)90582-5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1548697-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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