Research workbench
Structure of the P368G mutant of PMM/PGM from P. aeruginosa
Analyse Structure of the P368G mutant of PMM/PGM from P. aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C04
- Type
- protein
- Length
- 458 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE
- EC
- 5.4.2.8, 5.4.2.2
- UniProt
- P26276
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE (EC 5.4.2.8, 5.4.2.2) | protein | 458 | 38% helix, 24% strand | P26276 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 635 | 0.69 | 0.78 | 64 | empty |
| 2 | 105 | 0.47 | 0.80 | 18 | empty |
| 3 | 61 | 0.28 | 0.74 | 14 | empty |
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 3C04 · Structure of the P368G mutant of PMM/PGM from P. aeruginosa · the same entry in another collection · chain A against A, TM-score 1.00
- P26276 · AlphaFold monomer V2.0 prediction for PHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE (P26276) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P26276
- Elsewhere: RCSB PDB 3C04 · PDBe 3C04 · UniProt P26276
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