MolNFT v1 · #115410 · protein

Ran GDP wild type monoclinic crystal form

5CIT · GTP-binding nuclear protein ran: “Ran GDP wild type monoclinic crystal form”. X-ray diffraction, 2 ligands (GDP, MG), 1 pocket (best druggability 0.69). MolNFT v1 #115410 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5CIT
Type: protein
Length: 396 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTP-binding nuclear protein ran
UniProt: P62826
Ligands: GDP, MG
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GTP-binding nuclear protein ran	protein	199	34% helix, 28% strand	P62826
B	GTP-binding nuclear protein ran	protein	197	32% helix, 28% strand	P62826

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	992	0.69	0.74	67	empty

Interfaces

1 interface between chains.

A–B · 215 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

5CIT · Ran GDP wild type monoclinic crystal form · the same entry in another collection · chain A against A, TM-score 1.00

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
Elsewhere: RCSB PDB 5CIT · PDBe 5CIT · UniProt P62826

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