Research workbench
Inosine monophosphate dehydrogenase (impdh) from tritrichomonas foetus with xmp and mycophenolic acid bound
Analyse Inosine monophosphate dehydrogenase (impdh) from tritrichomonas foetus with xmp… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MEI
- Type
- protein
- Length
- 351 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inosine-5'-monophosphate dehydrogenase
- EC
- 1.1.1.205
- UniProt
- P50097
- Ligands
- XMP, MOA, K
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 351 | 36% helix, 20% strand | P50097 |
Ligands and binding sites
- XMP · Xanthosine-5'-monophosphate · ligand · chains A
- MOA · Mycophenolic acid · ligand · chains A
- K · Potassium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 583 | 0.77 | 0.84 | 58 | XMP, MOA |
| 2 | 75 | 0.35 | 0.76 | 15 | empty |
| 3 | 67 | 0.30 | 0.75 | 18 | empty |
| 4 | 63 | 0.27 | 0.72 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1MEI · Inosine Monophosphate Dehydrogenase (IMPDH) From Tritrichomonas Foetus with XMP and… · the same entry in another collection · chain A against A, TM-score 1.00
- P50097 · AlphaFold monomer V2.0 prediction for inosine-5'-monophosphate dehydrogenase (P50097) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P50097
- Elsewhere: RCSB PDB 1MEI · PDBe 1MEI · UniProt P50097
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