MolNFT v1 · #68943 · protein
Crystal structure of the nucleotide-binding protein AF_226 in complex with ADP from archaeoglobus fulgidus, northeast structural genomics consortium target GR157
3KB1: “Crystal structure of the nucleotide-binding protein AF_226 in complex with ADP from archaeoglobus fulgidus…”. X-ray diffraction, 2 ligands (ADP, ZN), 1 pocket (best druggability 0.79). MolNFT v1 #68943 on GenesisL1: 3D structure…
- PDB
- 3KB1
- Type
- protein
- Length
- 486 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleotide-binding protein
- UniProt
- O28015
- Ligands
- ADP, ZN
- Pockets
- 1 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Nucleotide-binding protein | protein | 243 | 32% helix, 25% strand | O28015 |
Ligands and binding sites
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 | 983 | 0.79 | 0.80 | 70 | ADP |
Interfaces
1 interface between chains.
- A–B · 873 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 3KB1 · Crystal Structure of the Nucleotide-binding protein AF_226 in complex with ADP 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 O28015
- Elsewhere: RCSB PDB 3KB1 · PDBe 3KB1 · UniProt O28015
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.