MolNFT v1 · #159026 · protein
The nucleotide-binding protein AF_226 in complex with ADP from archaeoglobus fulgidus with co found by pixe. based on 3KB1.
6OBY · Iron-sulfur cluster carrier protein: “The nucleotide-binding protein AF_226 in complex with ADP from archaeoglobus fulgidus with co found by pixe.…”. X-ray diffraction, 2 ligands (ADP, CO), 1 pocket (best druggability 0.79). MolNFT…
- PDB
- 6OBY
- Type
- protein
- Length
- 486 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Iron-sulfur cluster carrier protein
- UniProt
- O28015
- Ligands
- ADP, CO
- Pockets
- 1 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Iron-sulfur cluster carrier protein | protein | 243 | 34% helix, 24% strand | O28015 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- CO · Cobalt (II) ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 988 | 0.79 | 0.81 | 64 | ADP |
Interfaces
1 interface between chains.
- A–B · 849 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 6OBY · The nucleotide-binding protein AF_226 in complex with ADP from Archaeoglobus fulgidus… · 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 O28015
- Elsewhere: RCSB PDB 6OBY · PDBe 6OBY · UniProt O28015
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