MolNFT v1 · #25770 · protein
Structure of the bifunctional ispdf from campylobacter jejuni
1W55 · ISPD/ISPF bifunctional enzyme: “Structure of the bifunctional ispdf from campylobacter jejuni”. X-ray diffraction, 3 ligands (C, GPP, MG), 5 pockets (best druggability 0.55). MolNFT v1 #25770 on GenesisL1: 3D structure, binding…
- PDB
- 1W55
- Type
- protein
- Length
- 369 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ISPD/ISPF bifunctional enzyme
- EC
- 2.7.7.60, 4.6.1.12
- UniProt
- Q9PM68
- Ligands
- C, GPP, MG
- Pockets
- 5 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ISPD/ISPF bifunctional enzyme (EC 2.7.7.60, 4.6.1.12) | protein | 369 | 31% helix, 28% strand | Q9PM68 |
Ligands and binding sites
- C · Cytidine-5'-monophosphate · ligand · 2 copies · chains A
- GPP · Geranyl diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · chains A
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 | 236 | 0.55 | 0.78 | 32 | C |
| 2 | 60 | 0.38 | 0.79 | 11 | empty |
| 3 | 53 | 0.34 | 0.78 | 12 | empty |
| 4 | 59 | 0.29 | 0.74 | 15 | empty |
| 5 | 69 | 0.28 | 0.73 | 12 | empty |
Compared structures
- 1W55 · Structure of the Bifunctional IspDF from Campylobacter jejuni · the same entry in another collection · chain A against A, TM-score 1.00
- Q9PM68 · AlphaFold monomer V2.0 prediction for bifunctional enzyme ISPD/ISPF (Q9PM68) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q9PM68
- Elsewhere: RCSB PDB 1W55 · PDBe 1W55 · UniProt Q9PM68
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