Research workbench
Structure of mycobacterial maltokinase, the missing link in the essential glge-pathway (appcp complex)
Analyse Structure of mycobacterial maltokinase, the missing link in the essential… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4U98
- Type
- protein
- Length
- 451 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltokinase
- EC
- 2.7.1.175
- UniProt
- A1TH50
- Ligands
- ACP, MG
- Pockets
- 7 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltokinase (EC 2.7.1.175) | protein | 451 | 44% helix, 24% strand | A1TH50 |
Ligands and binding sites
- ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 152 | 0.65 | 0.87 | 33 | empty |
| 2 | 416 | 0.65 | 0.78 | 52 | ACP |
| 3 | 289 | 0.58 | 0.78 | 23 | empty |
| 4 | 140 | 0.47 | 0.78 | 23 | empty |
| 5 | 77 | 0.44 | 0.81 | 18 | empty |
Compared structures
- 4U98 · Structure of mycobacterial maltokinase, the missing link in the essential GlgE-pathway… · the same entry in another collection · chain A against A, TM-score 1.00
- A1TH50 · AlphaFold monomer V2.0 prediction for maltokinase (A1TH50) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 A1TH50
- Elsewhere: RCSB PDB 4U98 · PDBe 4U98 · UniProt A1TH50
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