Research workbench
Crystal structure of bacillus subtilis probable glutaminase, APC1040
Analyse Crystal structure of bacillus subtilis probable glutaminase, APC1040 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MKI
- Type
- protein
- Length
- 624 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable glutaminase ybgj
- EC
- 3.5.1.2
- UniProt
- O31465
- Pockets
- 6 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Probable glutaminase ybgj (EC 3.5.1.2) | protein | 312 | 49% helix, 13% strand | O31465 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 481 | 0.64 | 0.77 | 56 | empty |
| 2 | 200 | 0.48 | 0.75 | 28 | empty |
| 3 | 227 | 0.47 | 0.74 | 32 | empty |
| 4 | 142 | 0.45 | 0.76 | 14 | EDO |
| 5 | 98 | 0.39 | 0.76 | 14 | EDO |
Interfaces
1 interface between chains.
- A–B · 1234 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 26 modified (engineered, phosphorylation).
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 O31465
- Elsewhere: RCSB PDB 1MKI · PDBe 1MKI · UniProt O31465
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.