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Crystal structure of human full-length vinculin-T12-A974K (residues 1- 1066)

Analyse Crystal structure of human full-length vinculin-T12-A974K (residues 1- 1066) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FUY
Type: protein
Length: 961 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vinculin
UniProt: P18206
Ligands: CA
Pockets: 14 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vinculin	protein	961	78% helix, 0% strand	P18206

Ligands and binding sites

CA · Calcium ion · metal · chains A

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

Pockets

14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1006	0.81	0.82	97	empty
2	480	0.73	0.82	37	empty
3	384	0.67	0.80	50	empty
4	373	0.65	0.80	42	empty
5	139	0.52	0.80	27	empty

Compared structures

6FUY · Crystal structure of human full-length vinculin-T12-A974K (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 A 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 6FUY · PDBe 6FUY · UniProt P18206

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