Research workbench
Structure of the BIR1 domain of CIAP2
Analyse Structure of the BIR1 domain of CIAP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NK0
- Type
- protein
- Length
- 148 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Baculoviral iap repeat-containing protein 3
- EC
- 2.3.2.27
- UniProt
- Q13489
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, E | Baculoviral iap repeat-containing protein 3 (EC 2.3.2.27) | protein | 74 | 20% helix, 11% strand | Q13489 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.29 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- D–E · 276 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q13489
- Elsewhere: RCSB PDB 7NK0 · PDBe 7NK0 · UniProt Q13489
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