MolNFT v1 · #18051 · protein
Enzyme-ligand complex of P. aeruginosa PMM/PGM
1PCJ · Phosphomannomutase: “Enzyme-ligand complex of P. aeruginosa PMM/PGM”. X-ray diffraction, 2 ligands (M1P, ZN), 4 pockets (best druggability 0.69). MolNFT v1 #18051 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1PCJ
- Type
- protein
- Length
- 458 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphomannomutase
- EC
- 5.4.2.8
- UniProt
- P26276
- Ligands
- M1P, ZN
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Phosphomannomutase (EC 5.4.2.8) | protein | 458 | 38% helix, 24% strand | P26276 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 349 | 0.69 | 0.82 | 50 | M1P |
| 2 | 107 | 0.47 | 0.80 | 17 | empty |
| 3 | 72 | 0.40 | 0.79 | 20 | empty |
| 4 | 68 | 0.34 | 0.76 | 17 | empty |
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
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 1PCJ · PDBe 1PCJ · UniProt P26276
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