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Crystal structure of the methylimidazole-bound bjfixl heme domain
Analyse Crystal structure of the methylimidazole-bound bjfixl heme domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LSX
- Type
- protein
- Length
- 116 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor protein fixl
- EC
- 2.7.3.-
- UniProt
- P23222
- Ligands
- HEM, 1MZ
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensor protein fixl (EC 2.7.3.-) | protein | 116 | 36% helix, 36% strand | P23222 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- 1MZ · 1-methylimidazole · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 324 | 0.75 | 0.86 | 30 | HEM, 1MZ |
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 1LSX · PDBe 1LSX · UniProt P23222
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