MolNFT v1 · #82747 · protein

Crystal structure of CEX1P

3VWA · Cytoplasmic export protein 1: “Crystal structure of CEX1P”. X-ray diffraction, 7 pockets (best druggability 0.62). MolNFT v1 #82747 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3VWA
Type: protein
Length: 1,060 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytoplasmic export protein 1
UniProt: Q12453
Pockets: 7 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 63% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytoplasmic export protein 1	protein	531	62% helix, 8% strand	Q12453
B	Cytoplasmic export protein 1	protein	529	63% helix, 9% strand	Q12453

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	137	0.62	0.86	33	empty
2	143	0.55	0.81	33	empty
3	68	0.51	0.85	17	empty
4	66	0.51	0.85	17	empty
5	185	0.48	0.76	30	empty

Interfaces

1 interface between chains.

A–B · 69 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 modified (engineered).

Compared structures

3VWA · Crystal structure of Cex1p · the same entry in another collection · chain B against B, TM-score 1.00
Q12453 · AlphaFold monomer V2.0 prediction for cytoplasmic export protein 1 (Q12453) · a predicted model of the same protein · chain B 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 Q12453
Elsewhere: RCSB PDB 3VWA · PDBe 3VWA · UniProt Q12453

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