Research workbench
The crystal structure of a hydrolase from lactobacillus brevis
Analyse The crystal structure of a hydrolase from lactobacillus brevis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MPO
- Type
- protein
- Length
- 996 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Predicted hydrolase of the had superfamily
- UniProt
- Q03T33
- Pockets
- 11 · best druggability 0.61
Structure
x-ray diffraction · 4 distinct chains · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Predicted hydrolase of the had superfamily | protein | 240 | 40% helix, 23% strand | Q03T33 |
| B | Predicted hydrolase of the had superfamily | protein | 266 | 41% helix, 23% strand | Q03T33 |
| C | Predicted hydrolase of the had superfamily | protein | 257 | 40% helix, 24% strand | Q03T33 |
| D | Predicted hydrolase of the had superfamily | protein | 233 | 38% helix, 24% strand | Q03T33 |
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 318 | 0.61 | 0.79 | 42 | empty |
| 2 | 240 | 0.55 | 0.77 | 44 | empty |
| 3 | 164 | 0.53 | 0.80 | 26 | empty |
| 4 | 243 | 0.53 | 0.76 | 31 | empty |
| 5 | 146 | 0.52 | 0.80 | 25 | empty |
Interfaces
6 interfaces between chains.
- A–B · 790 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 782 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 781 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 780 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 96 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 32 modified (engineered).
Compared structures
- 3MPO · The crystal structure of a hydrolase from Lactobacillus brevis · 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 Q03T33
- Elsewhere: RCSB PDB 3MPO · PDBe 3MPO · UniProt Q03T33
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