Research workbench
IAP antagonist-induced conformational change in cIAP1 promotes E3 ligase activation via dimerization
Analyse IAP antagonist-induced conformational change in cIAP1 promotes E3 ligase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3T6P
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.897
- Source
- Homo sapiens
- Molecule
- Baculoviral IAP repeat-containing protein 2
- UniProt
- Q13490
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · resolution 1.897 · 1 distinct chain · 55% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Baculoviral IAP repeat-containing protein 2 | protein | 330 | 55% helix, 7% strand | Q13490 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.69 | 0.97 | 17 | empty |
| 2 | 320 | 0.60 | 0.78 | 38 | empty |
| 3 | 347 | 0.59 | 0.77 | 29 | empty |
| 4 | 123 | 0.55 | 0.82 | 23 | empty |
| 5 | 130 | 0.39 | 0.74 | 23 | empty |
Compared structures
- 3T6P · Iap antagonist-induced conformational change in CIAP1 promotes E3 ligase activation via… · the same entry in another collection · chain A against A, TM-score 1.00
- Q13490 · AlphaFold monomer V2.0 prediction for baculoviral iap repeat- containing protein 2… · a predicted model of the same protein · chain A against A, TM-score 0.99
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
- Elsewhere: RCSB PDB 3T6P · PDBe 3T6P · UniProt Q13490
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