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Crystal structure of human rangdp-NUP153ZNF2 complex

Analyse Crystal structure of human rangdp-NUP153ZNF2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GJ3
Type: protein
Length: 229 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTP-binding nuclear protein ran; Nuclear pore complex protein NUP153
UniProt: P62826, P49791
Ligands: GDP, MG, ZN

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GTP-binding nuclear protein ran	protein	202	34% helix, 27% strand	P62826
B	Nuclear pore complex protein NUP153	protein	27	0% helix, 22% strand	P49791

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
ZN · Zinc ion · metal · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

A–B · 472 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

3GJ3 · Crystal structure of human RanGDP-Nup153ZnF2 complex · the same entry in another collection · chain A against A, TM-score 1.00
P49791 · AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP153 (P49791) · a predicted model of the same protein · chain B against A, TM-score 0.83

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P62826
Every structure of UniProt P49791
Elsewhere: RCSB PDB 3GJ3 · PDBe 3GJ3 · UniProt P62826 · UniProt P49791

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