Research workbench
Crystal structure of the catalytic domain of inosine monophosphate dehydrogenase (impdh) from methanocaldococcus jannaschii
Analyse Crystal structure of the catalytic domain of inosine monophosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7XLO
- Type
- protein
- Length
- 650 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inosine-5'-monophosphate dehydrogenase
- EC
- 1.1.1.205
- UniProt
- Q59011
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 326 | 36% helix, 21% strand | Q59011 |
| B | Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 324 | 35% helix, 20% strand | Q59011 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 872 | 0.73 | 0.77 | 90 | empty |
| 2 | 348 | 0.72 | 0.84 | 39 | empty |
| 3 | 394 | 0.68 | 0.81 | 44 | empty |
| 4 | 110 | 0.37 | 0.74 | 19 | empty |
| 5 | 95 | 0.36 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 204 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 7XLO · Crystal Structure of the Catalytic Domain of Inosine Monophosphate Dehydrogenase (IMPDH)… · the same entry in another collection · chain A against A, TM-score 1.00
- Q59011 · AlphaFold monomer V2.0 prediction for inosine-5'-monophosphate dehydrogenase (Q59011) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q59011
- Elsewhere: RCSB PDB 7XLO · PDBe 7XLO · UniProt Q59011
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