Research workbench
Crystal structure of the catalytic domain of the inosine monophosphate dehydrogenase from listeria monocytogenes in the presence of xanthosine monophosphate
Analyse Crystal structure of the catalytic domain of the inosine monophosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UPX
- Type
- protein
- Length
- 380 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
- Q926Y9
- Ligands
- XMP
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 380 | 34% helix, 21% strand | Q926Y9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 625 | 0.79 | 0.85 | 67 | XMP |
| 2 | 279 | 0.55 | 0.76 | 25 | empty |
| 3 | 139 | 0.46 | 0.77 | 18 | empty |
| 4 | 138 | 0.43 | 0.76 | 25 | empty |
| 5 | 63 | 0.30 | 0.74 | 16 | empty |
Compared structures
- 5UPX · Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from… · 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 Q926Y9
- Elsewhere: RCSB PDB 5UPX · PDBe 5UPX · UniProt Q926Y9
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