MolNFT v1 · #30543 · protein
Crystal structure of the N-terminal, dimerization domain of siah interacting protein
2A26 · Calcyclin-binding protein: “Crystal structure of the N-terminal, dimerization domain of siah interacting protein”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.40). MolNFT v1 #30543 on GenesisL1: 3D structure…
- PDB
- 2A26
- Type
- protein
- Length
- 140 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcyclin-binding protein
- UniProt
- Q9HB71
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calcyclin-binding protein | protein | 48 | 85% helix, 0% strand | Q9HB71 |
| B, C | Calcyclin-binding protein | protein | 46 | 80% helix, 0% strand | Q9HB71 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.40 | 0.80 | 14 | empty |
| 2 | 66 | 0.31 | 0.75 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 910 Ų buried · 27 hydrogen bonds · protein-protein
- B–C · 408 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 336 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 2A26 · Crystal structure of the N-terminal, dimerization domain of Siah Interacting Protein · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HB71 · AlphaFold monomer V2.0 prediction for calcyclin-binding protein (Q9HB71) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 Q9HB71
- Elsewhere: RCSB PDB 2A26 · PDBe 2A26 · UniProt Q9HB71
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