MolNFT v1 · #2782 · protein
Staphylokinase (sak) dimer
1C77: “Staphylokinase (sak) dimer”. X-ray diffraction, 2 pockets (best druggability 0.51). MolNFT v1 #2782 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1C77
- 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
- 2 · best druggability 0.51
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, 46% strand | P68802 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 228 | 0.51 | 0.76 | 37 | empty |
| 2 | 72 | 0.35 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 570 Ų buried · 5 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 1C77 · PDBe 1C77 · UniProt P68802
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