MolNFT v2 · #79587 · protein
IAP antagonist-induced conformational change in cIAP1 promotes E3 ligase activation via dimerization
3T6P: “IAP antagonist-induced conformational change in cIAP1 promotes E3 ligase activation via dimerization”. X-ray diffraction at 1.897. MolNFT v2 #79587 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
- UniProt
- Q13490
Structure
x-ray diffraction · resolution 1.897 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 330 | — | Q13490 |
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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