Research workbench
Crystal structure of thermus caldophilus phosphoglycerate kinase in the open conformation
Analyse Crystal structure of thermus caldophilus phosphoglycerate kinase in the open… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IE8
- Type
- protein
- Length
- 390 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglycerate kinase
- EC
- 2.7.2.3
- UniProt
- Q08GC7
- Pockets
- 3 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglycerate kinase (EC 2.7.2.3) | protein | 390 | 42% helix, 17% strand | Q08GC7 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.48 | 0.75 | 33 | empty |
| 2 | 129 | 0.39 | 0.74 | 37 | empty |
| 3 | 59 | 0.27 | 0.73 | 10 | empty |
Compared structures
- 2IE8 · Crystal structure of Thermus caldophilus phosphoglycerate kinase in the open conformation · 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 Q08GC7
- Elsewhere: RCSB PDB 2IE8 · PDBe 2IE8 · UniProt Q08GC7
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