Research workbench
Crystal structure of phosphoglucomutase from leishmania major at 3.5 ångström resolution
Analyse Crystal structure of phosphoglucomutase from leishmania major at 3.5 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QG5
- Type
- protein
- Length
- 2,244 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative phosphoglucomutase
- EC
- 5.4.2.2
- UniProt
- Q4QCF1
- Ligands
- MG
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 28% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative phosphoglucomutase (EC 5.4.2.2) | protein | 565 | 30% helix, 19% strand | Q4QCF1 |
| B, D | Putative phosphoglucomutase (EC 5.4.2.2) | protein | 559 | 27% helix, 21% strand | Q4QCF1 |
| C | Putative phosphoglucomutase (EC 5.4.2.2) | protein | 561 | 28% helix, 21% strand | Q4QCF1 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 505 | 0.80 | 0.87 | 63 | empty |
| 2 | 860 | 0.76 | 0.79 | 73 | empty |
| 3 | 947 | 0.75 | 0.78 | 89 | empty |
| 4 | 649 | 0.75 | 0.81 | 83 | empty |
| 5 | 941 | 0.75 | 0.78 | 82 | empty |
Interfaces
5 interfaces between chains.
- A–D · 1044 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 990 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 778 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 268 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 220 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4QG5 · Crystal structure of phosphoglucomutase from Leishmania major at 3.5 angstrom resolution · 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 Q4QCF1
- Elsewhere: RCSB PDB 4QG5 · PDBe 4QG5 · UniProt Q4QCF1
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