Research workbench
Crystal structure of the alanine racemase BSU17640 from bacillus subtilis in the presence of bis-tris propane
Analyse Crystal structure of the alanine racemase BSU17640 from bacillus subtilis in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Q71
- Type
- protein
- Length
- 772 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alanine racemase 2
- UniProt
- A0A386RMP5
- Ligands
- PLP, MG, CL
- Pockets
- 10 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alanine racemase 2 | protein | 386 | 34% helix, 26% strand | A0A386RMP5 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 3 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 198 | 0.78 | 0.93 | 54 | PLP, CL |
| 2 | 297 | 0.78 | 0.89 | 48 | MG |
| 3 | 241 | 0.76 | 0.90 | 54 | PLP, CL |
| 4 | 133 | 0.49 | 0.79 | 28 | empty |
| 5 | 132 | 0.46 | 0.78 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 3154 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor, 2 disulfide (pyridoxal phosphate Schiff base, disulfide).
Compared structures
- 6Q71 · Crystal structure of the alanine racemase Bsu17640 from Bacillus subtilis in the presence… · 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 A0A386RMP5
- Elsewhere: RCSB PDB 6Q71 · PDBe 6Q71 · UniProt A0A386RMP5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.