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Crystal structure of human Pirin in complex with bisamide compound 2
Analyse Crystal structure of human Pirin in complex with bisamide compound 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H1I
- Type
- protein
- Length
- 287 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.69
- Source
- Homo sapiens
- Molecule
- Pirin
- EC
- 1.13.11.24
- UniProt
- O00625
- Ligands
- FJH, FE
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · resolution 1.69 · 1 distinct chain · 8% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pirin (EC 1.13.11.24) | protein | 287 | 8% helix, 49% strand | O00625 |
Ligands and binding sites
- FJH · ~{N}-[5-(2,3-dihydro-1,4-benzodioxin-6-ylcarbonylamino)-2-methyl-phenyl]-2-methyl-quinoline-6-carboxamide · ligand · chains A
- FE · Fe (III) ion · metal · chains A
- GOL · Glycerol · additive · 3 copies · 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 | 150 | 0.67 | 0.88 | 31 | FJH |
| 2 | 54 | 0.28 | 0.74 | 17 | GOL |
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 O00625
- Elsewhere: RCSB PDB 6H1I · PDBe 6H1I · UniProt O00625
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