› 2omd

X-ray diffraction
2Å resolution

Crystal structure of molybdopterin converting factor subunit 2 (aq_2181) from aquifex aeolicus VF5

Released:
DOI: 10.2210/pdb2omd/pdb
PDB entry 2omd coloured by chain, front view.
PDB entry 2omd coloured by chain, side view.
PDB entry 2omd coloured by chain, top view.
Source organism: Aquifex aeolicus VF5
Entry authors: Jeyakanthan J, Kanaujia SP, Vasuki Ranjani C, Sekar K, Agari Y, Ebihara A, Kuramitsu S, Shinkai A, Shiro Y, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed: 
Cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + H(2)O = molybdopterin + 2 [molybdopterin-synthase sulfur-carrier protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130589 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Molybdopterin synthase catalytic subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 154 amino acids
Theoretical weight: 17.61 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
  • Canonical: O67928 (Residues: 1-154; Coverage: 100%)
Gene names: aq_2181, moaE
Sequence domains: MoaE protein
Structure domains: Molybdopterin biosynthesis MoaE subunit

Ligands and Environments

5 bound ligands:
Ligand NA 2 x NA
Ligand CL 1 x CL
Ligand TRS 1 x TRS
Ligand FMT 2 x FMT
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P6122
Unit cell:
a: 119.995Å b: 119.995Å c: 125.804Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.19 0.215
Expression system: Escherichia coli

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