› 7mnz

X-ray diffraction
2.35Å resolution

Crystal Structure of Nup358/RanBP2 Ran-binding domain 4 in complex with Ran-GPPNHP

Released:
DOI: 10.2210/pdb7mnz/pdb
PDB entry 7mnz coloured by chain, front view.
PDB entry 7mnz coloured by chain, side view.
PDB entry 7mnz coloured by chain, top view.
Source organism: Homo sapiens
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-156036 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
GTP-binding nuclear protein Ran Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
Length: 216 amino acids
Theoretical weight: 24.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62826 (Residues: 1-215; Coverage: 100%)
Gene names: ARA24, OK/SW-cl.81, RAN
Sequence domains: Ras family
E3 SUMO-protein ligase RanBP2 Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 139 amino acids
Theoretical weight: 16.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49792 (Residues: 2911-3045; Coverage: 4%)
Gene names: NUP358, RANBP2
Sequence domains: RanBP1 domain

Ligands and Environments

2 bound ligands:
Ligand GNP 6 x GNP
Ligand MG 6 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P31
Unit cell:
a: 142.69Å b: 142.69Å c: 96.65Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.183 0.225
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