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Crystal structure of TL1A

Analyse Crystal structure of TL1A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O0O
Type: protein
Length: 458 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TNF superfamily ligand TL1A
UniProt: Q8NFE9
Ligands: MG
Pockets: 6 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 2% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	TNF superfamily ligand TL1A	protein	153	2% helix, 48% strand	Q8NFE9
C	TNF superfamily ligand TL1A	protein	152	2% helix, 51% strand	Q8NFE9

Ligands and binding sites

MG · Magnesium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	310	0.85	0.95	43	empty
2	76	0.58	0.88	17	empty
3	84	0.31	0.73	23	empty
4	61	0.29	0.74	19	empty
5	58	0.29	0.74	16	empty

Interfaces

3 interfaces between chains.

A–B · 1088 Å² buried · 11 hydrogen bonds · protein-protein
B–C · 1068 Å² buried · 16 hydrogen bonds · protein-protein
A–C · 1026 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

2O0O · Crystal structure of TL1A · 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 Q8NFE9
Elsewhere: RCSB PDB 2O0O · PDBe 2O0O · UniProt Q8NFE9

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