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Il-18RBETA tir domain

Analyse Il-18RBETA tir domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7FCH
Type: protein
Length: 572 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Interleukin-18 receptor accessory protein
EC: 3.2.2.6
UniProt: O95256
Pockets: 7 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Interleukin-18 receptor accessory protein (EC 3.2.2.6)	protein	143	44% helix, 17% strand	O95256

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	608	0.71	0.79	61	empty
2	388	0.62	0.77	46	empty
3	332	0.57	0.76	39	empty
4	275	0.56	0.76	30	empty
5	84	0.36	0.76	17	empty

Interfaces

3 interfaces between chains.

B–D · 688 Å² buried · 5 hydrogen bonds · protein-protein
A–C · 582 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 343 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

7FCH · IL-18Rbeta TIR domain · the same entry in another collection · chain A against A, TM-score 1.00
O95256 · AlphaFold monomer V2.0 prediction for interleukin-18 receptor accessory protein (O95256) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 O95256
Elsewhere: RCSB PDB 7FCH · PDBe 7FCH · UniProt O95256

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