MolNFT v2 · #150060 · protein
003 TCR Study of CDR Loop Flexibility
6FR4: “003 TCR Study of CDR Loop Flexibility”. X-ray diffraction at 1.28. MolNFT v2 #150060 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6FR4
- Type
- protein
- Length
- 445 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.28
- Source
- Homo sapiens
- UniProt
- Q6NSA1
Structure
x-ray diffraction · resolution 1.28 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 202 | — | Q6NSA1 |
| B | — | protein | 243 | — | — |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 15 copies · chains A, B
- GOL · Glycerol · additive · 6 copies · chains A, B
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6FR4 · 003 TCR study of cdr loop flexibility · 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 Q6NSA1
- Elsewhere: RCSB PDB 6FR4 · PDBe 6FR4 · UniProt Q6NSA1
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