MolNFT v1 · #11964 · protein
Siah, seven in absentia homolog
1K2F · Siah-1A protein: “Siah, seven in absentia homolog”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.35). MolNFT v1 #11964 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1K2F
- Type
- protein
- Length
- 380 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Siah-1A protein
- UniProt
- P61092
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Siah-1A protein | protein | 190 | 20% helix, 41% strand | P61092 |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A, B
- BME · Beta-mercaptoethanol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 97 | 0.35 | 0.74 | 22 | empty |
| 2 | 50 | 0.35 | 0.79 | 15 | empty |
| 3 | 54 | 0.29 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1173 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent (additive adduct).
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 P61092
- Elsewhere: RCSB PDB 1K2F · PDBe 1K2F · UniProt P61092
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