Research workbench
2-oxoquinoline 8-monooxygenase component: active site modulation by rieske-[2FE-2S] center OXIDATION/REDUCTION
Analyse 2-oxoquinoline 8-monooxygenase component: active site modulation by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z02
- Type
- protein
- Length
- 2,562 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2-oxo-1,2-dihydroquinoline 8-monooxygenase, oxygenase component
- EC
- 1.14.13.61
- UniProt
- O05935
- Ligands
- FES, FE
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | 2-oxo-1,2-dihydroquinoline 8-monooxygenase, oxygenase component (EC 1.14.13.61) | protein | 427 | 25% helix, 27% strand | O05935 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · 6 copies · chains A, B, C, D, E, F
- FE · Fe (III) ion · metal · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.81 | 0.91 | 36 | empty |
| 2 | 329 | 0.81 | 0.91 | 39 | empty |
| 3 | 320 | 0.81 | 0.91 | 38 | empty |
| 4 | 312 | 0.81 | 0.91 | 38 | FE |
| 5 | 305 | 0.80 | 0.91 | 39 | empty |
Interfaces
8 interfaces between chains.
- B–C · 2255 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 2244 Ų buried · 20 hydrogen bonds · protein-protein
- E–F · 2243 Ų buried · 23 hydrogen bonds · protein-protein
- D–E · 2233 Ų buried · 22 hydrogen bonds · protein-protein
- A–C · 2223 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 1Z02 · 2-Oxoquinoline 8-Monooxygenase Component: Active site Modulation by Rieske-[2fe-2S]… · the same entry in another collection · chain F against F, 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
- Every structure of UniProt O05935
- Elsewhere: RCSB PDB 1Z02 · PDBe 1Z02 · UniProt O05935
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