Research workbench
NMR structure of a 9 residue peptide from SMAC/DIABLO complexed to the BIR3 domain of xiap
Analyse NMR structure of a 9 residue peptide from SMAC/DIABLO complexed to the BIR3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G3F
- Type
- protein
- Length
- 126 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inhibitor of apoptosis protein 3; Smac
- UniProt
- P98170, Q9NR28
- Ligands
- ZN
Structure
solution nmr · 2 distinct chains · 33% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inhibitor of apoptosis protein 3 | protein | 117 | 35% helix, 8% strand | P98170 |
| B | Smac | protein | 9 | 0% helix, 22% strand | Q9NR28 |
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 · 316 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1G3F · NMR structure of a 9 residue peptide from SMAC/DIABLO complexed to the BIR3 domain of xiap · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NR28 · AlphaFold monomer V2.0 prediction for diablo homolog, mitochondrial (Q9NR28) · a predicted model of the same protein · chain B against A, TM-score 0.40
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 P98170
- Every structure of UniProt Q9NR28
- Elsewhere: RCSB PDB 1G3F · PDBe 1G3F · UniProt P98170 · UniProt Q9NR28
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.