Research workbench
Octameric mcsb from bacillus subtilis.
Analyse Octameric mcsb from bacillus subtilis. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TV6
- Type
- protein
- Length
- 1,418 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein-arginine kinase
- EC
- 2.7.14.1
- UniProt
- P37570
- Ligands
- MG
- Pockets
- 14 · best druggability 0.82
Structure
x-ray diffraction · 4 distinct chains · 50% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-arginine kinase (EC 2.7.14.1) | protein | 362 | 51% helix, 17% strand | P37570 |
| B | Protein-arginine kinase (EC 2.7.14.1) | protein | 353 | 49% helix, 18% strand | P37570 |
| C | Protein-arginine kinase (EC 2.7.14.1) | protein | 352 | 49% helix, 18% strand | P37570 |
| D | Protein-arginine kinase (EC 2.7.14.1) | protein | 351 | 50% helix, 18% strand | P37570 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1029 | 0.82 | 0.84 | 115 | empty |
| 2 | 236 | 0.80 | 0.93 | 44 | empty |
| 3 | 624 | 0.78 | 0.83 | 93 | empty |
| 4 | 188 | 0.76 | 0.92 | 38 | empty |
| 5 | 647 | 0.74 | 0.81 | 71 | empty |
Interfaces
4 interfaces between chains.
- A–B · 927 Ų buried · 22 hydrogen bonds · protein-protein
- B–C · 920 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 916 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 884 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (nonstandard).
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 P37570
- Elsewhere: RCSB PDB 6TV6 · PDBe 6TV6 · UniProt P37570
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