MolNFT v1 · #70334 · protein
The crystal structure of cbs domain protein from shewanella oneidensis mr-1.
3LHH: “The crystal structure of cbs domain protein from shewanella oneidensis mr-1.”. X-ray diffraction, 1 ligand (AMP), 1 pocket (best druggability 0.38). MolNFT v1 #70334 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3LHH
- Type
- protein
- Length
- 125 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cbs domain protein
- UniProt
- Q8EDE1
- Ligands
- AMP
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cbs domain protein | protein | 125 | 36% helix, 25% strand | Q8EDE1 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 77 | 0.38 | 0.77 | 16 | AMP |
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 3LHH · The crystal structure of CBS domain protein from Shewanella oneidensis MR-1. · 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 Q8EDE1
- Elsewhere: RCSB PDB 3LHH · PDBe 3LHH · UniProt Q8EDE1
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