Research workbench
Human BIR3 domain of Baculoviral Inhibitor of Apoptosis Repeat- Containing 3 (BIRC3)
Analyse Human BIR3 domain of Baculoviral Inhibitor of Apoptosis Repeat- Containing 3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2UVL
- Type
- protein
- Length
- 189 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.91
- Source
- HOMO SAPIENS
- Molecule
- Baculoviral iap repeat-containing protein 3
- UniProt
- Q13489
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · resolution 1.91 · 2 distinct chains · 46% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Baculoviral iap repeat-containing protein 3 | protein | 94 | 45% helix, 15% strand | Q13489 |
| B | Baculoviral iap repeat-containing protein 3 | protein | 95 | 46% helix, 12% strand | Q13489 |
Ligands and binding sites
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 | 213 | 0.67 | 0.85 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 1004 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 2UVL · Human BIR3 domain of baculoviral inhibitor of apoptosis repeat- containing 3 (BIRC3) · the same entry in another collection · chain A against A, TM-score 1.00
- Q13489 · AlphaFold monomer V2.0 prediction for baculoviral iap repeat- containing protein 3… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q13489
- Elsewhere: RCSB PDB 2UVL · PDBe 2UVL · UniProt Q13489
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