Research workbench
Co-bound structure of bjfixlh
Analyse Co-bound structure of bjfixlh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XJ4
- Type
- protein
- Length
- 213 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor protein fixl
- EC
- 2.7.3.-
- UniProt
- P23222
- Ligands
- HEM, NA, CMO, CL
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensor protein fixl (EC 2.7.3.-) | protein | 106 | 28% helix, 39% strand | P23222 |
| B | Sensor protein fixl (EC 2.7.3.-) | protein | 107 | 26% helix, 38% strand | P23222 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A
- CMO · Carbon monoxide · ion · 2 copies · chains A, B
- CL · Chloride ion · ion · 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 | 337 | 0.79 | 0.88 | 31 | HEM, CMO |
| 2 | 290 | 0.78 | 0.89 | 32 | HEM, CMO |
| 3 | 136 | 0.45 | 0.77 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 733 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
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 P23222
- Elsewhere: RCSB PDB 1XJ4 · PDBe 1XJ4 · UniProt P23222
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