Research workbench
Crystal structure of fold bifunctional protein from campylobacter jejuni
Analyse Crystal structure of fold bifunctional protein from campylobacter jejuni in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P2O
- Type
- protein
- Length
- 566 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional protein fold
- EC
- 1.5.1.5, 3.5.4.9
- UniProt
- Q0PA35
- Ligands
- NAD
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional protein fold (EC 1.5.1.5, 3.5.4.9) | protein | 284 | 42% helix, 17% strand | Q0PA35 |
| B | Bifunctional protein fold (EC 1.5.1.5, 3.5.4.9) | protein | 282 | 43% helix, 17% strand | Q0PA35 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.72 | 0.98 | 16 | GOL |
| 2 | 446 | 0.67 | 0.78 | 47 | NAD |
| 3 | 452 | 0.66 | 0.78 | 41 | NAD |
| 4 | 104 | 0.34 | 0.73 | 23 | empty |
| 5 | 65 | 0.31 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1750 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 modified (engineered).
Compared structures
- 3P2O · Crystal Structure of FolD Bifunctional Protein from Campylobacter jejuni · the same entry in another collection · chain A against A, TM-score 1.00
- Q0PA35 · AlphaFold monomer V2.0 prediction for bifunctional protein fold (Q0PA35) · 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 Q0PA35
- Elsewhere: RCSB PDB 3P2O · PDBe 3P2O · UniProt Q0PA35
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