Research workbench
Crystal structure of the marr family transcriptional regulator from variovorax paradoxus bound to catechol
Analyse Crystal structure of the marr family transcriptional regulator from variovorax… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KK0
- Type
- protein
- Length
- 135 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator, marr family
- UniProt
- C5CSP2
- Ligands
- CAQ, SO4
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator, marr family | protein | 135 | 74% helix, 9% strand | C5CSP2 |
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 | 501 | 0.62 | 0.75 | 30 | CAQ |
Compared structures
- 7KK0 · Crystal structure of the MarR family transcriptional regulator from Variovorax paradoxus… · 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 C5CSP2
- Elsewhere: RCSB PDB 7KK0 · PDBe 7KK0 · UniProt C5CSP2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.