› 3mch

X-ray diffraction
1.64Å resolution

Crystal structure of the molybdopterin biosynthesis enzyme MoaB (TTHA0341) from thermus theromophilus HB8

Released:
DOI: 10.2210/pdb3mch/pdb
PDB entry 3mch coloured by chain, front view.
PDB entry 3mch coloured by chain, side view.
PDB entry 3mch coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Crystal structures, dynamics and functional implications of molybdenum-cofactor biosynthesis protein MogA from two thermophilic organisms.
Kanaujia SP, Jeyakanthan J, Shinkai A, Kuramitsu S, Yokoyama S, Sekar K
Acta Crystallogr Sect F Struct Biol Cryst Commun 67 2-16 (2011)
PMID: 21206014

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178163 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MoaB/Mog domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 164 amino acids
Theoretical weight: 17.88 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SLF2 (Residues: 1-164; Coverage: 100%)
Gene name: TTHA0341
Sequence domains: Probable molybdopterin binding domain
Structure domains: MoaB/Mog-like domain

Ligands and Environments

1 bound ligand:
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P21
Unit cell:
a: 33.935Å b: 103.316Å c: 59.592Å
α: 90° β: 101.33° γ: 90°
R-values:
R R work R free
0.192 0.192 0.217
Expression system: Escherichia coli

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Citations

1 review citation

Experimental evidence validating the computational inference of functional associations from gene fusion events: a critical survey.
Promponas et al. (2014)
1 other article

2 mentions without citation

Crystal structures, dynamics and functional implications of molybdenum-cofactor biosynthesis protein MogA from two thermophilic organisms.
Kanaujia et al. (2011)
1 more