Research workbench
Crystal structure of CIAP1 BIR3 bound to GDC0152
Analyse Crystal structure of CIAP1 BIR3 bound to GDC0152 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UW4
- Type
- protein
- Length
- 90 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Baculoviral iap repeat-containing protein 2, baculoviral iap repeat-containing protein 4…
- UniProt
- Q13490, P98170
- Ligands
- 0DQ, ZN
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Baculoviral iap repeat-containing protein 2, baculoviral iap repeat-containing protein 4 | protein | 87 | 43% helix, 10% strand | Q13490, P98170 |
| Z | GDC0152 | protein | 3 | 0% helix, 33% strand | — |
Ligands and binding sites
- 0DQ · 4-phenyl-1,2,3-thiadiazol-5-amine · ligand · chains A, Z
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–Z · 278 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified, 1 covalent (nonstandard, covalent ligand).
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 Q13490
- Every structure of UniProt P98170
- Elsewhere: RCSB PDB 3UW4 · PDBe 3UW4 · UniProt Q13490 · UniProt P98170
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