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Structure of tim-3 in complex with phosphatidylserine

Analyse Structure of tim-3 in complex with phosphatidylserine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KAA
Type: protein
Length: 216 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hepatitis a virus cellular receptor 2
UniProt: Q3KP82
Ligands: PSF, CA
Pockets: 1 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hepatitis a virus cellular receptor 2	protein	107	6% helix, 37% strand	Q3KP82
B	Hepatitis a virus cellular receptor 2	protein	109	6% helix, 41% strand	Q3KP82

Ligands and binding sites

PSF · 1,2-dicaproyl-sn-phosphatidyl-L-serine · ligand · chains A, B
CA · Calcium ion · metal · chains B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	360	0.60	0.77	53	CA, PSF

Interfaces

1 interface between chains.

A–B · 317 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

3KAA · Structure of Tim-3 in complex with phosphatidylserine · the same entry in another collection · chain A 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 Q3KP82
Elsewhere: RCSB PDB 3KAA · PDBe 3KAA · UniProt Q3KP82

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