2nq2

X-ray diffraction
2.4Å resolution

An inward-facing conformation of a putative metal-chelate type ABC transporter.

Released:

Function and Biology Details

Reaction catalysed:
ATP + H(2)O + molybdate-[molybdate-binding protein](Side 1) = ADP + phosphate + molybdate(Side 2) + [molybdate-binding protein](Side 1)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-176403 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Molybdate import system permease protein MolB Chains: A, B
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 36.55 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q57130 (Residues: 1-337; Coverage: 100%)
Gene names: HI_1471, molB
Sequence domains: FecCD transport family
Structure domains: ABC transporter involved in vitamin B12 uptake, BtuC
Molybdate import ATP-binding protein MolC Chains: C, D
Molecule details ›
Chains: C, D
Length: 253 amino acids
Theoretical weight: 28.55 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q57399 (Residues: 1-253; Coverage: 100%)
Gene names: HI_1470, molC
Sequence domains: ABC transporter
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 97.846Å b: 142.465Å c: 150.268Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.222 0.26
Expression system: Escherichia coli