› 7mo5

X-ray diffraction
1.55Å resolution

Crystal Structure of the ZnF4 of Nucleoporin NUP153 in complex with Ran-GDP

Released:
DOI: 10.2210/pdb7mo5/pdb
PDB entry 7mo5 coloured by chain, front view.
PDB entry 7mo5 coloured by chain, side view.
PDB entry 7mo5 coloured by chain, top view.
Source organisms:
Entry authors: Bley CJ, Nie S, Mobbs GW, Petrovic S, Gres AT, Liu X, Mukherjee S, Harvey S, Huber FM, Lin DH, Brown B, Tang AW, Rundlet EJ, Correia AR, Chen S, Regmi SG, Stevens TA, Jette CA, Dasso M, Patke A, Palazzo AF, Kossiakoff AA, Hoelz A

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156032 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
GTP-binding nuclear protein Ran Chain: A
Molecule details ›
Chain: A
Length: 217 amino acids
Theoretical weight: 24.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62826 (Residues: 1-216; Coverage: 100%)
Gene names: ARA24, OK/SW-cl.81, RAN
Sequence domains: Ras family
Nuclear pore complex protein Nup153 Chain: B
Molecule details ›
Chain: B
Length: 42 amino acids
Theoretical weight: 4.46 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P49791 (Residues: 838-874; Coverage: 3%)
Gene name: Nup153
Sequence domains: Zn-finger in Ran binding protein and others

Ligands and Environments

3 bound ligands:
Ligand GDP 1 x GDP
Ligand MG 1 x MG
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P21212
Unit cell:
a: 59.78Å b: 80.11Å c: 54.48Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.162 0.19
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Electron microscopy holdings of the Protein Data Bank: the impact of the resolution revolution, new validation tools, and implications for the future.
Burley et al. (2022)
8 more