MolNFT v1 · #148892 · protein
Xray structure of domain-swapped cystatin E dimer
6FK0 · Cystatin-M: “Xray structure of domain-swapped cystatin E dimer”. X-ray diffraction, 1 pocket (best druggability 0.30). MolNFT v1 #148892 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6FK0
- Type
- protein
- Length
- 224 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cystatin-M
- UniProt
- Q15828
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cystatin-M | protein | 113 | 20% helix, 50% strand | Q15828 |
| B | Cystatin-M | protein | 111 | 21% helix, 50% strand | Q15828 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.30 | 0.75 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 3512 Ų buried · 61 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (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 Q15828
- Elsewhere: RCSB PDB 6FK0 · PDBe 6FK0 · UniProt Q15828
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