Research workbench
003 TCR Study of CDR Loop Flexibility
Analyse 003 TCR Study of CDR Loop Flexibility in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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
- Molecule
- TCR 003 alpha chain; TCR 003 Beta Chain
- UniProt
- Q6NSA1
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · resolution 1.28 · 2 distinct chains · 6% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TCR 003 alpha chain | protein | 202 | 5% helix, 46% strand | Q6NSA1 |
| B | TCR 003 Beta Chain | protein | 243 | 7% helix, 49% strand | — |
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.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 875 | 0.72 | 0.77 | 86 | EDO |
| 2 | 57 | 0.34 | 0.77 | 15 | empty |
| 3 | 58 | 0.30 | 0.74 | 13 | empty |
| 4 | 55 | 0.29 | 0.75 | 15 | GOL, EDO |
| 5 | 58 | 0.27 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2194 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
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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