› 5mss

X-ray diffraction
1.96Å resolution

Structure of the A-PCP didomain of carboxylic acid reductase (CAR) from Segniliparus rugosus in complex with AMP

Released:
DOI: 10.2210/pdb5mss/pdb
PDB entry 5mss coloured by chain, front view.
PDB entry 5mss coloured by chain, side view.
PDB entry 5mss coloured by chain, top view.
Source organism: Segniliparus rugosus ATCC BAA-974
Primary publication:
Structures of carboxylic acid reductase reveal domain dynamics underlying catalysis.
Gahloth D, Dunstan MS, Quaglia D, Klumbys E, Lockhart-Cairns MP, Hill AM, Derrington SR, Scrutton NS, Turner NJ, Leys D
Nat Chem Biol 13 975-981 (2017)
PMID: 28719588

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123014 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxylic acid reductase Chain: A
Molecule details ›
Chain: A
Length: 1188 amino acids
Theoretical weight: 128.37 KDa
Source organism: Segniliparus rugosus ATCC BAA-974
Expression system: Escherichia coli
UniProt:
  • Canonical: E5XP76 (Residues: 1-1188; Coverage: 100%)
Gene names: HMPREF9336_01297, car
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand AMP 1 x AMP
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2221
Unit cell:
a: 59.719Å b: 127.693Å c: 212.244Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.204 0.254
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Biocatalysis: Enzymatic Synthesis for Industrial Applications.
Wu et al. (2021)
9 more

6 mentions without citation

From Protein Film Electrochemistry to Nanoconfined Enzyme Cascades and the Electrochemical Leaf.
Armstrong et al. (2023)
5 more