Research workbench
The X-ray structure of ferric escherichia COLI flavohemoglobin reveals an unespected geometry of the distal heme pocket
Analyse The X-ray structure of ferric escherichia COLI flavohemoglobin reveals an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GVH
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flavohemoprotein
- EC
- 1.6.99.7
- UniProt
- P24232
- Ligands
- FAD, HEM, NA, CL
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flavohemoprotein (EC 1.6.99.7) | protein | 396 | 45% helix, 19% strand | P24232 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- NA · Sodium ion · metal · 2 copies · chains A
- CL · Chloride ion · 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 | 1044 | 0.82 | 0.83 | 86 | FAD, HEM, NA, CL |
| 2 | 119 | 0.43 | 0.77 | 22 | empty |
Compared structures
- 1GVH · The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unespected… · the same entry in another collection · chain A against A, TM-score 1.00
- P24232 · AlphaFold monomer V2.0 prediction for flavohemoprotein (P24232) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P24232
- Elsewhere: RCSB PDB 1GVH · PDBe 1GVH · UniProt P24232
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