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Crystal structure of HSALC1
Analyse Crystal structure of HSALC1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EPU
- Type
- protein
- Length
- 978 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non-immunized human scfv; Chromodomain-helicase-DNA-binding protein 1-like
- EC
- 3.6.4.12
- UniProt
- Q86WJ1
- Ligands
- ADP, MG
- Pockets
- 19 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Non-immunized human scfv | protein | 230 | 5% helix, 50% strand | — |
| B | Chromodomain-helicase-DNA-binding protein 1-like (EC 3.6.4.12) | protein | 748 | 41% helix, 11% strand | Q86WJ1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.73 | 0.97 | 18 | empty |
| 2 | 610 | 0.73 | 0.80 | 84 | ADP, MG |
| 3 | 64 | 0.68 | 0.95 | 24 | empty |
| 4 | 388 | 0.64 | 0.78 | 36 | empty |
| 5 | 277 | 0.62 | 0.80 | 39 | empty |
Interfaces
1 interface between chains.
- A–B · 1349 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent, 2 disulfide (covalent ligand, 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 Q86WJ1
- Elsewhere: RCSB PDB 7EPU · PDBe 7EPU · UniProt Q86WJ1
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