Research workbench
Crystal structure of the human TRIP12 wwe domain (isoform 2) in complex with ADP
Analyse Crystal structure of the human TRIP12 wwe domain (isoform 2) in complex with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7UW7
- Type
- protein
- Length
- 72 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 2 of E3 ubiquitin-protein ligase TRIP12
- EC
- 2.3.2.26
- Ligands
- ADP, UNX
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform 2 of E3 ubiquitin-protein ligase TRIP12 (EC 2.3.2.26) | protein | 72 | 17% helix, 46% strand | — |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- UNX · Unknown atom or ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 7UW7 · PDBe 7UW7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.