MolNFT v1 · #90867 · protein
Study on structure and function relationships in human pirin with mn ion
4EWD: “Study on structure and function relationships in human pirin with mn ion”. X-ray diffraction, 1 ligand (MN), 2 pockets (best druggability 0.65). MolNFT v1 #90867 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4EWD
- Type
- protein
- Length
- 288 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
- MN
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pirin (EC 1.13.11.24) | protein | 288 | 8% helix, 49% strand | O00625 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 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 | 172 | 0.65 | 0.85 | 31 | empty |
| 2 | 55 | 0.30 | 0.76 | 18 | 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 4EWD · PDBe 4EWD · UniProt O00625
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