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Cryogenic electron microscopy model of full-length human metavinculin

Analyse Cryogenic electron microscopy model of full-length human metavinculin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7KTT
Type
protein
Length
994 residues
Chains
1
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Metavinculin
UniProt
P18206
Pockets
16 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 76% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMetavinculinprotein99476% helix, 0% strandP18206

Pockets

16 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16210.800.8688empty
23030.780.8932empty
31430.770.9427empty
4770.710.9524empty
51310.690.9037empty

Compared structures

  • 7KTT · Cryogenic electron microscopy model of full-length human metavinculin · 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 0.95

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