Research workbench
E69 deletion mutant single insulin-like growth factor binding domain protein (sibd-1) from cupiennius salei
Analyse E69 deletion mutant single insulin-like growth factor binding domain protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZXC
- Type
- protein
- Length
- 145 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Single insulin-like growth factor-binding domain protein-1
- UniProt
- G4V4F9
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Single insulin-like growth factor-binding domain protein-1 | protein | 71 | 8% helix, 32% strand | G4V4F9 |
| B | Single insulin-like growth factor-binding domain protein-1 | protein | 74 | 8% helix, 31% strand | G4V4F9 |
Ligands and binding sites
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 634 | 0.81 | 0.86 | 63 | ACT |
Interfaces
1 interface between chains.
- A–B · 912 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 3ZXC · E69 deletion mutant single insulin-like growth factor binding domain protein (SIBD-1)… · the same entry in another collection · chain A against A, TM-score 1.00
- G4V4F9 · AlphaFold monomer V2.0 prediction for single insulin-like growth factor-binding domain… · a predicted model of the same protein · chain B against A, TM-score 0.97
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 G4V4F9
- Elsewhere: RCSB PDB 3ZXC · PDBe 3ZXC · UniProt G4V4F9
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