PDBe 3ve1

X-ray diffraction
2.96Å resolution

The 2.9 angstrom crystal structure of Transferrin binding protein B (TbpB) from serogroup B M982 Neisseria meningitidis in complex with human transferrin

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transferrin-binding protein 2 Chains: A, C
Molecule details ›
Chains: A, C
Length: 658 amino acids
Theoretical weight: 71.41 KDa
Source organism: Neisseria meningitidis serogroup B
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q09057 (Residues: 56-711; Coverage: 95%)
Gene names: tbp2, tbpB
Sequence domains:
Structure domains:
Serotransferrin Chains: B, D
Molecule details ›
Chains: B, D
Length: 679 amino acids
Theoretical weight: 75.29 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P02787 (Residues: 20-698; Coverage: 100%)
Gene names: PRO1400, TF
Sequence domains: Transferrin
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 128.023Å b: 153.509Å c: 169.511Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.249
Expression systems:
  • Escherichia coli BL21(DE3)
  • Komagataella pastoris