MolNFT v1 · #14990 · protein
The crystal structure of alpha-D-glucuronidase from bacillus stearothermophilus T-6
1MQP: “The crystal structure of alpha-D-glucuronidase from bacillus stearothermophilus T-6”. X-ray diffraction, 4 pockets (best druggability 0.65). MolNFT v1 #14990 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MQP
- Type
- protein
- Length
- 669 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-D-glucuronidase
- EC
- 3.2.1.139
- UniProt
- Q8VVD2
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-D-glucuronidase (EC 3.2.1.139) | protein | 669 | 39% helix, 13% strand | Q8VVD2 |
Ligands and binding sites
- GOL · Glycerol · additive · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 452 | 0.65 | 0.78 | 38 | GOL |
| 2 | 154 | 0.49 | 0.78 | 22 | empty |
| 3 | 76 | 0.47 | 0.82 | 16 | GOL |
| 4 | 72 | 0.39 | 0.78 | 13 | empty |
Compared structures
- 1MQP · The crystal structure of alpha-D-glucuronidase from bacillus stearothermophilus T-6 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q8VVD2
- Elsewhere: RCSB PDB 1MQP · PDBe 1MQP · UniProt Q8VVD2
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