Research workbench
Human transthyretin (ttr) complexed with quercetin 3-O-beta-D- galactoside
Analyse Human transthyretin (ttr) complexed with quercetin 3-O-beta-D- galactoside in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Z60
- Type
- protein
- Length
- 231 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02766
- Ligands
- J6O
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 116 | — | P02766 |
| B | — | protein | 115 | — | P02766 |
Ligands and binding sites
- J6O · 2-[3,4-bis(oxidanyl)phenyl]-3-[(2S,3R,4S,5R,6R)-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-5,7-bis(oxidanyl)chromen-4-one · ligand · chains B
- EDO · 1,2-ethanediol · additive · chains A, B
- IMD · Imidazole · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7Z60 · Human transthyretin (TTR) complexed with Quercetin 3-O-beta-D-galactoside · 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 7Z60 · PDBe 7Z60 · UniProt P02766
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