Research workbench
2.4 a resolution crystal structure of borrelia burgdorferi inosine 5'- monphosphate dehydrogenase in complex with a sulfate ion
Analyse 2.4 a resolution crystal structure of borrelia burgdorferi inosine 5'… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EEP
- Type
- protein
- Length
- 628 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
- P49058
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inosine 5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 314 | 37% helix, 19% strand | P49058 |
| B | Inosine 5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 314 | 34% helix, 19% strand | P49058 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 284 | 0.52 | 0.75 | 36 | SO4 |
| 2 | 212 | 0.49 | 0.75 | 29 | SO4 |
| 3 | 62 | 0.31 | 0.76 | 18 | empty |
| 4 | 68 | 0.30 | 0.74 | 19 | empty |
| 5 | 61 | 0.27 | 0.73 | 15 | empty |
Compared structures
- 1EEP · 2.4 a resolution crystal structure of borrelia burgdorferi inosine 5'-monphosphate… · the same entry in another collection · chain A against A, TM-score 1.00
- P49058 · AlphaFold monomer V2.0 prediction for inosine-5'-monophosphate dehydrogenase (P49058) · a predicted model of the same protein · chain B 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 P49058
- Elsewhere: RCSB PDB 1EEP · PDBe 1EEP · UniProt P49058
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