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Crystal structure of the C-terminal calponin homology domain of alpha parvin

Analyse Crystal structure of the C-terminal calponin homology domain of alpha parvin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2VZC
Type
protein
Length
253 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-parvin
UniProt
Q9NVD7
Pockets
1 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 62% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-parvinprotein12761% helix, 0% strandQ9NVD7
BAlpha-parvinprotein12664% helix, 0% strandQ9NVD7

Ligands and binding sites

  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
  • GOL · Glycerol · additive · chains A
  • MRD · (4R)-2-methylpentane-2,4-diol · additive · chains A, B
  • MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13260.720.8543MRD, MPD

Interfaces

1 interface between chains.

  • A–B · 502 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 2VZC · Crystal structure of the C-terminal calponin homology domain of alpha parvin · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9NVD7 · AlphaFold monomer V2.0 prediction for alpha-parvin (Q9NVD7) · a predicted model of the same protein · chain B against A, TM-score 0.98

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