3gug

X-ray diffraction
1.9Å resolution

Crystal structure of AKR1C1 L308V mutant in complex with NADP and 3,5-dichlorosalicylic acid

Released:
Source organism: Homo sapiens
Entry authors: Dhagat U, El-Kabbani O

Function and Biology Details

Reactions catalysed:
Indan-1-ol + NAD(P)(+) = indanone + NAD(P)H
17-alpha,20-alpha-dihydroxypregn-4-en-3-one + NAD(P)(+) = 17-alpha-hydroxyprogesterone + NAD(P)H
Trans-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol + NADPH
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldo-keto reductase family 1 member C1 Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 36.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04828 (Residues: 1-323; Coverage: 100%)
Gene names: AKR1C1, DDH, DDH1
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 39.412Å b: 83.885Å c: 48.914Å
α: 90° β: 90.98° γ: 90°
R-values:
R R work R free
0.194 0.19 0.26
Expression system: Escherichia coli