Research workbench
Kuenenia stuttgartiensis reducing hao-like protein complex KUSTC0457/KUSTC0458
Analyse Kuenenia stuttgartiensis reducing hao-like protein complex KUSTC0457/KUSTC0458 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H5L
- Type
- protein
- Length
- 726 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Similar to hydroxylamine oxidoreductase; Conserved hypothetical cytochrome protein
- EC
- 1.7.3.4
- UniProt
- Q1PVE0, Q1PVE1
- Ligands
- HEC
- Pockets
- 9 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Similar to hydroxylamine oxidoreductase (EC 1.7.3.4) | protein | 506 | 55% helix, 3% strand | Q1PVE0 |
| B | Conserved hypothetical cytochrome protein | protein | 220 | 40% helix, 2% strand | Q1PVE1 |
Ligands and binding sites
- HEC · Heme C · ligand · 10 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 654 | 0.88 | 0.93 | 103 | HEC |
| 2 | 784 | 0.81 | 0.84 | 71 | HEC |
| 3 | 195 | 0.78 | 0.93 | 33 | HEC |
| 4 | 77 | 0.69 | 0.93 | 18 | empty |
| 5 | 56 | 0.61 | 0.92 | 15 | HEC |
Interfaces
1 interface between chains.
- A–B · 588 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 cofactor (heme c attachment).
Compared structures
- 6H5L · Kuenenia stuttgartiensis reducing HAO-like protein complex Kustc0457/Kustc0458 · 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
- Every structure of UniProt Q1PVE0
- Every structure of UniProt Q1PVE1
- Elsewhere: RCSB PDB 6H5L · PDBe 6H5L · UniProt Q1PVE0 · UniProt Q1PVE1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.