Research workbench
Crystal structure of HUTS-4 Fv-clasp fragment
Analyse Crystal structure of HUTS-4 Fv-clasp fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CEA
- Type
- protein
- Length
- 326 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.55
- Source
- Homo sapiens; Mus musculus
- Molecule
- Huts-4 VH(S112C)-sarah; Huts-4 VL(C87Y)-SARAH(S37C)
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · resolution 2.55 · 2 distinct chains · 27% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Huts-4 VH(S112C)-sarah | protein | 174 | 27% helix, 35% strand | — |
| B | Huts-4 VL(C87Y)-SARAH(S37C) | protein | 152 | 27% helix, 34% strand | — |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.50 | 0.77 | 23 | empty |
| 2 | 131 | 0.45 | 0.78 | 25 | empty |
| 3 | 50 | 0.28 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2627 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 7CEA · Crystal structure of huts-4 fv-clasp fragment · 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 7CEA · PDBe 7CEA
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