Research workbench
Crystal structure of DIAP1 BIR1 bound to a grim peptide
Analyse Crystal structure of DIAP1 BIR1 bound to a grim peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SE0
- Type
- protein
- Length
- 104 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apoptosis 1 inhibitor; Cell death protein grim
- UniProt
- Q24306
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Apoptosis 1 inhibitor | protein | 97 | 27% helix, 11% strand | Q24306 |
| B | Cell death protein grim | protein | 7 | 0% helix, 57% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 439 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1SE0 · Crystal structure of DIAP1 BIR1 bound to a Grim peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q24306 · AlphaFold monomer V2.0 prediction for death-associated inhibitor of apoptosis 1 (Q24306) · a predicted model of the same protein · chain A 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 Q24306
- Elsewhere: RCSB PDB 1SE0 · PDBe 1SE0 · UniProt Q24306
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