Research workbench

TNF receptor subtype one-selective TNF mutant with antagonistic activity; R1ANTTNF-T8

Analyse TNF receptor subtype one-selective TNF mutant with antagonistic activity… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZPX
Type: protein
Length: 426 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tumor necrosis factor
UniProt: P01375
Pockets: 7 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Tumor necrosis factor	protein	142	0% helix, 50% strand	P01375

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	82	0.78	0.99	21	empty
2	123	0.65	0.89	34	empty
3	141	0.57	0.82	23	empty
4	104	0.48	0.80	21	empty
5	102	0.46	0.79	29	empty

Interfaces

3 interfaces between chains.

B–C · 1158 Å² buried · 20 hydrogen bonds · protein-protein
A–C · 1155 Å² buried · 21 hydrogen bonds · protein-protein
A–B · 1145 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

2ZPX · TNF Receptor Subtype One-selective TNF Mutant with Antagonistic Activity; R1antTNF-T8 · 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 2ZPX · PDBe 2ZPX · UniProt P01375

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