MolNFT v1 · #2783 · protein
Staphylokinase (sak) dimer
1C78: “Staphylokinase (sak) dimer”. X-ray diffraction, 4 pockets (best druggability 0.56). MolNFT v1 #2783 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1C78
- Type
- protein
- Length
- 258 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Staphylokinase
- EC
- 3.4.24.29
- UniProt
- P68802
- Pockets
- 4 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Staphylokinase (EC 3.4.24.29) | protein | 130 | 9% helix, 37% strand | P68802 |
| B | Staphylokinase (EC 3.4.24.29) | protein | 128 | 9% helix, 45% strand | P68802 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 340 | 0.56 | 0.74 | 30 | empty |
| 2 | 65 | 0.49 | 0.85 | 17 | empty |
| 3 | 51 | 0.29 | 0.76 | 13 | empty |
| 4 | 70 | 0.27 | 0.72 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 525 Ų buried · 12 hydrogen bonds · protein-protein
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 P68802
- Elsewhere: RCSB PDB 1C78 · PDBe 1C78 · UniProt P68802
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