MolNFT v1 · #6613 · protein
Crystal structure of germin (oxalate oxidase)
1FI2: “Crystal structure of germin (oxalate oxidase)”. X-ray diffraction, 1 ligand (MN), 2 pockets (best druggability 0.45). MolNFT v1 #6613 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1FI2
- Type
- protein
- Length
- 201 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oxalate oxidase
- EC
- 1.2.3.4
- UniProt
- P45850
- Ligands
- MN
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxalate oxidase (EC 1.2.3.4) | protein | 201 | 17% helix, 30% strand | P45850 |
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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.45 | 0.81 | 28 | empty |
| 2 | 80 | 0.32 | 0.75 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P45850
- Elsewhere: RCSB PDB 1FI2 · PDBe 1FI2 · UniProt P45850
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