MolNFT v1 · #91931 · protein
The structure of a putative signal-transduction protein with cbs domains from burkholderia ambifaria MC40-6
4FRY: “The structure of a putative signal-transduction protein with cbs domains from burkholderia ambifaria MC40-6”. X-ray diffraction, 2 ligands (NAD, AMP), 3 pockets (best druggability 0.70). MolNFT v1 #91931 on GenesisL1: 3D structure…
- PDB
- 4FRY
- Type
- protein
- Length
- 274 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative signal-transduction protein with cbs domains
- UniProt
- B1YXI0
- Ligands
- NAD, AMP
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative signal-transduction protein with cbs domains | protein | 136 | 38% helix, 24% strand | B1YXI0 |
| B | Putative signal-transduction protein with cbs domains | protein | 138 | 39% helix, 23% strand | B1YXI0 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- AMP · Adenosine monophosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 494 | 0.70 | 0.80 | 55 | NAD, AMP |
| 2 | 460 | 0.69 | 0.80 | 48 | AMP, NAD |
| 3 | 58 | 0.26 | 0.72 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1491 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 4FRY · The structure of a putative signal-transduction protein with CBS domains 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 B1YXI0
- Elsewhere: RCSB PDB 4FRY · PDBe 4FRY · UniProt B1YXI0
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