MolNFT v1 · #23139 · protein

Crystal structure of human full-length vinculin (residues 1- 1066)

1TR2 · Vinculin isoform 1: “Crystal structure of human full-length vinculin (residues 1- 1066)”. X-ray diffraction, 20 pockets (best druggability 0.85). MolNFT v1 #23139 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1TR2
Type: protein
Length: 2,057 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vinculin isoform 1
UniProt: P18206
Pockets: 20 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 76% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vinculin isoform 1	protein	1028	76% helix, 1% strand	P18206
B	Vinculin isoform 1	protein	1029	75% helix, 1% strand	P18206

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	821	0.85	0.88	70	empty
2	604	0.81	0.87	56	empty
3	998	0.79	0.81	105	empty
4	1063	0.76	0.78	73	empty
5	355	0.75	0.86	44	empty

Interfaces

1 interface between chains.

A–B · 1400 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 72 modified (engineered).

Compared structures

1TR2 · Crystal structure of human full-length vinculin (residues 1-1066) · the same entry in another collection · chain A against A, TM-score 1.00
P18206 · AlphaFold monomer V2.0 prediction for vinculin (P18206) · a predicted model of the same protein · chain B 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 P18206
Elsewhere: RCSB PDB 1TR2 · PDBe 1TR2 · UniProt P18206

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