MolNFT v1 · #20622 · protein

Human vinculin head (1-258) in complex with human vinculin tail (879-1066)

1RKE: “Human vinculin head (1-258) in complex with human vinculin tail (879-1066)”. X-ray diffraction, 4 pockets (best druggability 0.59). MolNFT v1 #20622 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1RKE
Type: protein
Length: 438 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vinculin; Vcl protein
UniProt: P18206
Pockets: 4 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 74% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vinculin	protein	262	79% helix, 1% strand	P18206
B	Vcl protein	protein	176	66% 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	196	0.59	0.81	30	empty
2	99	0.41	0.77	22	empty
3	92	0.39	0.76	18	empty
4	51	0.37	0.80	13	empty

Interfaces

1 interface between chains.

A–B · 1390 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

1RKE · Human vinculin head (1-258) in complex with human vinculin tail (879-1066) · 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 1RKE · PDBe 1RKE · UniProt P18206

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