MolNFT v1 · #52387 · protein
Crystal structure of the C-terminal calponin homology domain of alpha parvin
2VZC · Alpha-parvin: “Crystal structure of the C-terminal calponin homology domain of alpha parvin”. X-ray diffraction, 1 pocket (best druggability 0.72). MolNFT v1 #52387 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-parvin | protein | 127 | 61% helix, 0% strand | Q9NVD7 |
| B | Alpha-parvin | protein | 126 | 64% helix, 0% strand | Q9NVD7 |
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 326 | 0.72 | 0.85 | 43 | MRD, 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
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 Q9NVD7
- Elsewhere: RCSB PDB 2VZC · PDBe 2VZC · UniProt Q9NVD7
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