Research workbench
Ferric soybean leghemoglobin complexed with nicotinate
Analyse Ferric soybean leghemoglobin complexed with nicotinate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FSL
- Type
- protein
- Length
- 286 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leghemoglobin a
- UniProt
- P02238
- Ligands
- HEM, NIO
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Leghemoglobin a | protein | 143 | 76% helix, 0% strand | P02238 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- NIO · Nicotinic acid · ligand · 2 copies · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 596 | 0.73 | 0.80 | 56 | empty |
| 2 | 346 | 0.71 | 0.83 | 29 | HEM, NIO |
| 3 | 305 | 0.70 | 0.83 | 30 | HEM, NIO |
Interfaces
1 interface between chains.
- A–B · 346 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 P02238
- Elsewhere: RCSB PDB 1FSL · PDBe 1FSL · UniProt P02238
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