MolNFT v1 · #161051 · protein
N-acetylmannosamine kinase from staphylococcus aureus
6Q26 · Glucokinase: “N-acetylmannosamine kinase from staphylococcus aureus”. X-ray diffraction, 13 pockets (best druggability 0.81). MolNFT v1 #161051 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6Q26
- Type
- protein
- Length
- 1,131 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucokinase
- EC
- 2.7.1.2, 2.7.1.85
- UniProt
- A0A266CX40
- Pockets
- 13 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, B | Glucokinase (EC 2.7.1.2, 2.7.1.85) | protein | 286 | 38% helix, 22% strand | A0A266CX40 |
| D | Glucokinase (EC 2.7.1.2, 2.7.1.85) | protein | 273 | 39% helix, 21% strand | A0A266CX40 |
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 385 | 0.81 | 0.90 | 39 | empty |
| 2 | 322 | 0.79 | 0.90 | 40 | empty |
| 3 | 316 | 0.77 | 0.89 | 54 | empty |
| 4 | 669 | 0.72 | 0.79 | 61 | empty |
| 5 | 657 | 0.71 | 0.78 | 61 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1591 Ų buried · 34 hydrogen bonds · protein-protein
- D–C · 1503 Ų buried · 36 hydrogen bonds · protein-protein
- C–B · 1102 Ų buried · 23 hydrogen bonds · protein-protein
- A–D · 1023 Ų buried · 22 hydrogen bonds · protein-protein
- D–B · 57 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 6Q26 · N-Acetylmannosamine kinase from Staphylococcus aureus · 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 A0A266CX40
- Elsewhere: RCSB PDB 6Q26 · PDBe 6Q26 · UniProt A0A266CX40
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