Research workbench

TIM-1

Analyse TIM-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OR8
Type: protein
Length: 232 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hepatitis a virus cellular receptor 1 homolog
UniProt: Q5QNS5
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hepatitis a virus cellular receptor 1 homolog	protein	116	5% helix, 41% strand	Q5QNS5

Ligands and binding sites

ACT · Acetate ion · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	704	0.68	0.76	60	empty
2	70	0.47	0.83	22	empty

Interfaces

1 interface between chains.

A–B · 548 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

2OR8 · Tim-1 · the same entry in another collection · chain A against A, TM-score 1.00
Q5QNS5 · AlphaFold monomer V2.0 prediction for hepatitis a virus cellular receptor 1 homolog… · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q5QNS5
Elsewhere: RCSB PDB 2OR8 · PDBe 2OR8 · UniProt Q5QNS5

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