Research workbench
Crystal structure of human pirin in complex with a chemical probe pyrrolidine 24
Analyse Crystal structure of human pirin in complex with a chemical probe pyrrolidine 24 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JCT
- Type
- protein
- Length
- 287 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pirin
- EC
- 1.13.11.24
- UniProt
- O00625
- Ligands
- 6JQ, FE
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pirin (EC 1.13.11.24) | protein | 287 | 8% helix, 48% strand | O00625 |
Ligands and binding sites
- 6JQ · N-{5-[(2,3-dihydro-1,4-benzodioxine-6-carbonyl)amino]-2-methylphenyl}-2-[3-(pyrrolidin-1-yl)propyl]quinoline-6-carboxamide · ligand · chains A
- FE · Fe (III) ion · metal · chains A
- DMS · Dimethyl sulfoxide · additive · 2 copies · chains A
- GOL · Glycerol · additive · 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 | 131 | 0.67 | 0.89 | 28 | 6JQ |
| 2 | 51 | 0.28 | 0.75 | 15 | empty |
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 5JCT · PDBe 5JCT · UniProt O00625
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