MolNFT v1 · #26429 · protein
Crystal structure of inorganic POLYPHOSPHATE/ATP-glucomannokinase from arthrobacter sp. strain km at 1.8 a resolution
1WOQ: “Crystal structure of inorganic POLYPHOSPHATE/ATP-glucomannokinase from arthrobacter sp. strain km at 1.8 a…”. X-ray diffraction, 2 ligands (BGC, PO4), 5 pockets (best druggability 0.72). MolNFT v1 #26429 on GenesisL1: 3D structure…
- PDB
- 1WOQ
- Type
- protein
- Length
- 506 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inorganic POLYPHOSPHATE/ATP-glucomannokinase
- EC
- 2.7.1.63
- UniProt
- Q7WT42
- Ligands
- BGC, PO4
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Inorganic POLYPHOSPHATE/ATP-glucomannokinase (EC 2.7.1.63) | protein | 253 | 38% helix, 27% strand | Q7WT42 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 370 | 0.72 | 0.84 | 51 | BGC, PO4 |
| 2 | 258 | 0.71 | 0.86 | 53 | BGC, PO4 |
| 3 | 245 | 0.51 | 0.75 | 33 | empty |
| 4 | 167 | 0.44 | 0.74 | 26 | empty |
| 5 | 63 | 0.31 | 0.75 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1190 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1WOQ · Crystal Structure of Inorganic Polyphosphate/ATP-Glucomannokinase From Arthrobacter sp.… · 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 Q7WT42
- Elsewhere: RCSB PDB 1WOQ · PDBe 1WOQ · UniProt Q7WT42
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