› 5msp

X-ray diffraction
2.41Å resolution

Structure of the unmodified PCP-R didomain of carboxylic acid reductase (CAR) from Segniliparus rugosus in complex with NADP, F2221 form

Released:
DOI: 10.2210/pdb5msp/pdb
PDB entry 5msp coloured by chain, front view.
PDB entry 5msp coloured by chain, side view.
PDB entry 5msp 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:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:
Ligand NAP 1 x NAP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: F222
Unit cell:
a: 135.37Å b: 137.68Å c: 202.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.179 0.227
Expression system: Escherichia coli

Quick links

Citations

11 review citations

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

6 mentions without citation

Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.
Patel et al. (2023)
5 more