MolNFT v2 · #171287 · protein

Crystal Structure of KPT-330 bound to CRM1 (E582K, 537-DLTVK-541 to GLCEQ)

6XJS: “Crystal Structure of KPT-330 bound to CRM1 (E582K, 537-DLTVK-541 to GLCEQ)”. X-ray diffraction at 1.942, 3 ligands (GNP, V6A, MG). MolNFT v2 #171287 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6XJS
Type: protein
Length: 1,342 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.942
Source: Homo sapiens; Saccharomyces cerevisiae
UniProt: P62826, P41920, P30822
Ligands: GNP, V6A, MG

Structure

x-ray diffraction · resolution 1.942 · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	208	—	P62826
B	—	protein	123	—	P41920
C	—	protein	1011	—	P30822

Ligands and binding sites

GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
V6A · selinexor, bound form · ligand · chains C
MG · Magnesium ion · metal · chains A
GOL · Glycerol · additive · 2 copies · chains C

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

Compared structures

6XJS · Crystal structure of kpt-330 bound to CRM1 (E582K, 537-dltvk-541 to glceq) · the same entry in another collection · chain A against A, TM-score 1.00
P41920 · AlphaFold monomer V2.0 prediction for ran-specific GTPase-activating protein 1 (P41920) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P41920
Every structure of UniProt P30822
Elsewhere: RCSB PDB 6XJS · PDBe 6XJS · UniProt P62826 · UniProt P41920 · UniProt P30822

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