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Crystal structure of phosphoglycerate kinase-2
Analyse Crystal structure of phosphoglycerate kinase-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2P9Q
- Type
- protein
- Length
- 807 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglycerate kinase, testis specific
- EC
- 2.7.2.3
- UniProt
- P09041
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglycerate kinase, testis specific (EC 2.7.2.3) | protein | 404 | 36% helix, 18% strand | P09041 |
| B | Phosphoglycerate kinase, testis specific (EC 2.7.2.3) | protein | 403 | 37% helix, 18% strand | P09041 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1139 | 0.74 | 0.77 | 84 | empty |
| 2 | 138 | 0.51 | 0.79 | 25 | empty |
| 3 | 120 | 0.45 | 0.78 | 25 | empty |
| 4 | 87 | 0.45 | 0.80 | 17 | empty |
| 5 | 107 | 0.41 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 472 Ų buried · 9 hydrogen bonds · protein-protein
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 P09041
- Elsewhere: RCSB PDB 2P9Q · PDBe 2P9Q · UniProt P09041
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