MolNFT v1 · #94008 · protein
Kinetic stabilization of transthyretin through covalent modification of K15 by (E)-N-(4-(4-hydroxy-3,5-DIMETHYLSTYRYL)PHENYL)PROPIONAMIDE
4HJT: “Kinetic stabilization of transthyretin through covalent modification of K15 by…”. X-ray diffraction. MolNFT v1 #94008 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4HJT
- Type
- protein
- Length
- 231 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02766
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 116 | — | P02766 |
| B | — | protein | 115 | — | P02766 |
Compared structures
- 4HJT · Kinetic stabilization of transthyretin through covalent modification of K15 by… · the same entry in another collection · chain A against A, TM-score 1.00
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 P02766
- Elsewhere: RCSB PDB 4HJT · PDBe 4HJT · UniProt P02766
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