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The structure of tumor necrosis factor-alpha at 2.6 ångströms resolution. implications for receptor binding

Analyse The structure of tumor necrosis factor-alpha at 2.6 ångströms resolution.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TNF
Type: protein
Length: 456 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tumor necrosis factor-alpha
UniProt: P01375
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Tumor necrosis factor-alpha	protein	152	2% helix, 44% strand	P01375

Pockets

2 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	255	0.76	0.89	32	empty
2	72	0.76	0.98	18	empty

Interfaces

3 interfaces between chains.

A–B · 1290 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 1198 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 1166 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1TNF · The structure of tumor necrosis factor-alpha at 2.6 ångströms resolution. implications… · 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 P01375
Elsewhere: RCSB PDB 1TNF · PDBe 1TNF · UniProt P01375

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