Research workbench
Globular domain of zebrafish complement 1QA protein
Analyse Globular domain of zebrafish complement 1QA protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HBA
- Type
- protein
- Length
- 386 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- F1QFM5
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.35
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 133 | 0% helix, 56% strand | F1QFM5 |
| B | Uncharacterized protein | protein | 127 | 0% helix, 57% strand | F1QFM5 |
| C | Uncharacterized protein | protein | 126 | 0% helix, 58% strand | F1QFM5 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.35 | 0.75 | 15 | empty |
| 2 | 53 | 0.33 | 0.76 | 12 | empty |
| 3 | 90 | 0.32 | 0.73 | 14 | empty |
| 4 | 75 | 0.28 | 0.72 | 14 | empty |
Interfaces
3 interfaces between chains.
- A–B · 839 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 836 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 827 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 5HBA · Globular Domain of Zebrafish Complement 1qA protein · 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 F1QFM5
- Elsewhere: RCSB PDB 5HBA · PDBe 5HBA · UniProt F1QFM5
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