› 2p91

X-ray diffraction
2Å resolution

Crystal structure of Enoyl-[acyl-carrier-protein] reductase (NADH) from Aquifex aeolicus VF5

Released:
DOI: 10.2210/pdb2p91/pdb
PDB 2p91 coloured by chain and viewed from the front.
PDB 2p91 coloured by chain and viewed from the side.
PDB 2p91 coloured by chain and viewed from the top.
Source organism: Aquifex aeolicus VF5
Entry authors: Chen L, Li Y, Ebihara A, Shinkai A, Kuramitsu S, Yokoyama S, Zhao M, Rose JP, Wang B-C, Southeast Collaboratory for Structural Genomics (SECSG), RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed: 
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 285 amino acids
Theoretical weight: 31.54 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
  • Canonical: O67505 (Residues: 1-270; Coverage: 100%)
Gene names: aq_1552, fabI
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 72.078Å b: 119.019Å c: 119.197Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.167 0.197
Expression system: Escherichia coli

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