Research workbench
N-acetylmannosamine kinase with N-acetylmannosamine from staphylococcus aureus
Analyse N-acetylmannosamine kinase with N-acetylmannosamine from staphylococcus aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Q27
- Type
- protein
- Length
- 1,140 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
- Ligands
- BM3
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Glucokinase (EC 2.7.1.2, 2.7.1.85) | protein | 285 | 38% helix, 22% strand | A0A266CX40 |
Ligands and binding sites
- BM3 · 2-acetamido-2-deoxy-alpha-D-mannopyranose · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 563 | 0.79 | 0.85 | 66 | BM3 |
| 2 | 630 | 0.79 | 0.84 | 72 | BM3 |
| 3 | 510 | 0.78 | 0.86 | 64 | BM3 |
| 4 | 605 | 0.78 | 0.84 | 69 | BM3 |
| 5 | 95 | 0.68 | 0.92 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1683 Ų buried · 37 hydrogen bonds · protein-protein
- A–C · 813 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 802 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6Q27 · N-acetylmannosamine kinase with N-acetylmannosamine 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 6Q27 · PDBe 6Q27 · UniProt A0A266CX40
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