MolNFT v1 · #25182 · protein
Crystal structure of ADP compounds hydrolase
1VHZ · ADP compounds hydrolase nude: “Crystal structure of ADP compounds hydrolase”. X-ray diffraction, 1 ligand (APR), 2 pockets (best druggability 0.82). MolNFT v1 #25182 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1VHZ
- Type
- protein
- Length
- 371 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP compounds hydrolase nude
- EC
- 3.6.1.-
- UniProt
- P45799
- Ligands
- APR
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP compounds hydrolase nude (EC 3.6.1.-) | protein | 186 | 20% helix, 44% strand | P45799 |
| B | ADP compounds hydrolase nude (EC 3.6.1.-) | protein | 185 | 19% helix, 45% strand | P45799 |
Ligands and binding sites
- APR · Adenosine-5-diphosphoribose · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1028 | 0.82 | 0.83 | 99 | APR |
| 2 | 52 | 0.33 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 2945 Ų buried · 47 hydrogen bonds · protein-protein
Compared structures
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 P45799
- Elsewhere: RCSB PDB 1VHZ · PDBe 1VHZ · UniProt P45799
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