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LMP1 protein binds to TRAF3 as a structural CD40

Analyse LMP1 protein binds to TRAF3 as a structural CD40 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZMS
Type: protein
Length: 199 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TNF receptor associated factor 3; Latent membrane protein 1
UniProt: Q13114, P13198
Pockets: 2 · best druggability 0.29

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	TNF receptor associated factor 3	protein	192	28% helix, 28% strand	Q13114
B	Latent membrane protein 1	protein	7	0% helix, 29% strand	P13198

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	72	0.29	0.73	15	empty
2	62	0.29	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 448 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1ZMS · LMP1 Protein binds to TRAF3 as a structural CD40 · the same entry in another collection · chain A against A, TM-score 1.00
Q13114 · AlphaFold monomer V2.0 prediction for TNF receptor-associated factor 3 (Q13114) · a predicted model of the same protein · chain A 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 Q13114
Every structure of UniProt P13198
Elsewhere: RCSB PDB 1ZMS · PDBe 1ZMS · UniProt Q13114 · UniProt P13198

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