Research workbench
Crystal structure of lmrr with bound copper phenanthroline
Analyse Crystal structure of lmrr with bound copper phenanthroline in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R1L
- Type
- protein
- Length
- 100 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator, padr-like family
- UniProt
- A2RI36
- Ligands
- PHN, CU
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 1 distinct chain · 66% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator, padr-like family | protein | 100 | 66% helix, 14% strand | A2RI36 |
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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.30 | 0.74 | 13 | empty |
Compared structures
- 6R1L · Crystal structure of LmrR with bound copper phenanthroline · 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 A2RI36
- Elsewhere: RCSB PDB 6R1L · PDBe 6R1L · UniProt A2RI36
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.