Research workbench
Ru-porphyrin protein scaffolds for sensing O2
Analyse Ru-porphyrin protein scaffolds for sensing O2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3M0B
- Type
- protein
- Length
- 185 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyl-accepting chemotaxis protein
- UniProt
- Q8RBX6
- Ligands
- RUR, CMO
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methyl-accepting chemotaxis protein | protein | 185 | 51% helix, 20% strand | Q8RBX6 |
Ligands and binding sites
- RUR · [3,3'-(7,12-diethyl-3,8,13,17-tetramethylporphyrin-2, 18-diyl-kappa~4~n~21~,n~22~,n~23~,n~24~) dipropanoato(2-)]ruthenium · ligand · chains A
- CMO · Carbon monoxide · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 365 | 0.83 | 0.91 | 35 | RUR, CMO |
| 2 | 82 | 0.36 | 0.75 | 17 | empty |
Compared structures
- 3M0B · Ru-Porphyrin Protein Scaffolds for Sensing O2 · 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 Q8RBX6
- Elsewhere: RCSB PDB 3M0B · PDBe 3M0B · UniProt Q8RBX6
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