Research workbench
Inosine monophosphate dehydrogenase (impdh; ec 1.1.1.205) from streptococcus pyogenes
Analyse Inosine monophosphate dehydrogenase (impdh; ec 1.1.1.205) from streptococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZFJ
- Type
- protein
- Length
- 476 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inosine monophosphate dehydrogenase
- EC
- 1.1.1.205
- UniProt
- P0C0H6
- Ligands
- IMP
- Pockets
- 7 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inosine monophosphate dehydrogenase (EC 1.1.1.205) | protein | 476 | 34% helix, 21% strand | P0C0H6 |
Ligands and binding sites
- IMP · Inosinic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 432 | 0.74 | 0.84 | 46 | IMP |
| 2 | 261 | 0.57 | 0.77 | 25 | empty |
| 3 | 182 | 0.54 | 0.79 | 24 | empty |
| 4 | 199 | 0.46 | 0.74 | 32 | empty |
| 5 | 131 | 0.44 | 0.76 | 17 | empty |
Modifications
Observed in the structure: 13 modified (engineered).
Compared structures
- 1ZFJ · Inosine monophosphate dehydrogenase (impdh; ec 1.1.1.205) from streptococcus pyogenes · the same entry in another collection · chain A against A, TM-score 1.00
- P0C0H6 · AlphaFold monomer V2.0 prediction for inosine-5'-monophosphate dehydrogenase (P0C0H6) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P0C0H6
- Elsewhere: RCSB PDB 1ZFJ · PDBe 1ZFJ · UniProt P0C0H6
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