MolNFT v2 · #151511 · protein

Crystal structure of the TNPO3 - CPSF6 RSLD complex

6GX9: “Crystal structure of the TNPO3 - CPSF6 RSLD complex”. X-ray diffraction at 2.7, 3 ligands (BCN, BEN, MG). MolNFT v2 #151511 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6GX9
Type: protein
Length: 1,841 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.7
Source: Homo sapiens
UniProt: Q9Y5L0, Q16630
Ligands: BCN, BEN, MG

Structure

x-ray diffraction · resolution 2.7 · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	912	—	Q9Y5L0
B	—	protein	911	—	Q9Y5L0
C, D	—	protein	9	—	Q16630

Ligands and binding sites

BCN · Bicine · ligand · 2 copies · chains A, B
BEN · Benzamidine · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 4 copies · chains A, B

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

Compared structures

6GX9 · Crystal structure of the TNPO3 - CPSF6 rsld complex · the same entry in another collection · chain D against D, TM-score 1.00
Q9Y5L0 · AlphaFold monomer V2.0 prediction for transportin-3 (Q9Y5L0) · a predicted model of the same protein · chain A against A, TM-score 0.99
Q16630 · AlphaFold monomer V2.0 prediction for cleavage and polyadenylation specificity factor… · a predicted model of the same protein · chain D against A, TM-score 0.43

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 Q9Y5L0
Every structure of UniProt Q16630
Elsewhere: RCSB PDB 6GX9 · PDBe 6GX9 · UniProt Q9Y5L0 · UniProt Q16630

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