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Human vinculin R903Q, D907R, R910T MUTANT(RESIDUES 891-1066)

Analyse Human vinculin R903Q, D907R, R910T MUTANT(RESIDUES 891-1066) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5L0J
Type: protein
Length: 331 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vinculin
UniProt: P18206
Pockets: 4 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 72% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vinculin	protein	165	73% helix, 1% strand	P18206
B	Vinculin	protein	166	70% helix, 2% strand	P18206

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	96	0.55	0.85	18	empty
2	178	0.48	0.76	20	empty
3	84	0.34	0.74	12	empty
4	73	0.34	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 703 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5L0J · Human vinculin R903Q, D907R, R910T mutant(residues 891-1066) · 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 0.97

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 5L0J · PDBe 5L0J · UniProt P18206

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