MolNFT v1 · #69546 · protein
Structural basis of GW182 recognition by POLY(A)-binding protein
3KTP · Polyadenylate-binding protein 1: “Structural basis of GW182 recognition by POLY(A)-binding protein”. X-ray diffraction. MolNFT v1 #69546 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3KTP
- Type
- protein
- Length
- 94 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyadenylate-binding protein 1; Trinucleotide repeat-containing gene 6C protein
- UniProt
- P11940, Q9HCJ0
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyadenylate-binding protein 1 | protein | 78 | 79% helix, 0% strand | P11940 |
| B | Trinucleotide repeat-containing gene 6C protein | protein | 16 | 0% helix, 0% strand | Q9HCJ0 |
Interfaces
1 interface between chains.
- A–B · 659 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3KTP · Structural basis of GW182 recognition by poly(A)-binding protein · the same entry in another collection · chain A against A, TM-score 1.00
- P11940 · AlphaFold monomer V2.0 prediction for polyadenylate-binding protein 1 (P11940) · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q9HCJ0 · AlphaFold monomer V2.0 prediction for trinucleotide repeat-containing gene 6C protein… · a predicted model of the same protein · chain B against A, TM-score 0.21
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 P11940
- Every structure of UniProt Q9HCJ0
- Elsewhere: RCSB PDB 3KTP · PDBe 3KTP · UniProt P11940 · UniProt Q9HCJ0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.