MolNFT v1 · #142461 · protein
Oxidase chap-H1
6A52 · Dioxidase chap-H1: “Oxidase chap-H1”. X-ray diffraction, 1 ligand (FE2), 2 pockets (best druggability 0.54). MolNFT v1 #142461 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6A52
- Type
- protein
- Length
- 249 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dioxidase chap-H1
- Ligands
- FE2
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dioxidase chap-H1 | protein | 124 | 23% helix, 37% strand | — |
| B | Dioxidase chap-H1 | protein | 125 | 22% helix, 33% strand | — |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.54 | 0.77 | 37 | FE2 |
| 2 | 220 | 0.52 | 0.77 | 41 | FE2 |
Interfaces
1 interface between chains.
- A–B · 1739 Ų buried · 37 hydrogen bonds · protein-protein
Compared structures
- 6A52 · Oxidase ChaP-H1 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 6A52 · PDBe 6A52
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