Research workbench
Structure of the protein kinase yabt from bacillus subtilis in complex with an alpharep crystallization helper
Analyse Structure of the protein kinase yabt from bacillus subtilis in complex with an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6G4J
- Type
- protein
- Length
- 395 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable SERINE/THREONINE-protein kinase yabt; Alpharep BE8
- EC
- 2.7.11.1
- UniProt
- P37562
- Pockets
- 6 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable SERINE/THREONINE-protein kinase yabt (EC 2.7.11.1) | protein | 273 | 41% helix, 23% strand | P37562 |
| B | Alpharep BE8 | protein | 122 | 80% helix, 0% strand | — |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 238 | 0.56 | 0.78 | 33 | empty |
| 2 | 208 | 0.54 | 0.78 | 30 | empty |
| 3 | 92 | 0.51 | 0.82 | 16 | empty |
| 4 | 115 | 0.39 | 0.75 | 18 | empty |
| 5 | 109 | 0.39 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 901 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 6G4J · Structure of the protein kinase YabT from Bacillus subtilis in complex with an alphaREP… · the same entry in another collection · chain A against A, TM-score 1.00
- P37562 · AlphaFold monomer V2.0 prediction for probable SERINE/THREONINE- protein kinase yabt… · a predicted model of the same protein · 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 P37562
- Elsewhere: RCSB PDB 6G4J · PDBe 6G4J · UniProt P37562
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