5ugj

X-ray diffraction
2.7Å resolution

Crystal structure of HTPA Reductase from neisseria meningitidis

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-191739 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 302 amino acids
Theoretical weight: 32.14 KDa
Source organism: Neisseria meningitidis MC58
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9K1F1 (Residues: 1-269; Coverage: 100%)
Gene names: NMB0203, dapB
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P21
Unit cell:
a: 69.866Å b: 66.748Å c: 133.535Å
α: 90° β: 105.12° γ: 90°
R-values:
R R work R free
0.209 0.206 0.25
Expression system: Escherichia coli