Research workbench
Structure of the btla ectodomain
Analyse Structure of the btla ectodomain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XAU
- Type
- protein
- Length
- 104 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- B- and T-lymphocyte attenuator
- UniProt
- Q7TSA3
- Ligands
- CD
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | B- and T-lymphocyte attenuator | protein | 104 | 3% helix, 53% strand | Q7TSA3 |
Ligands and binding sites
- CD · Cadmium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 Q7TSA3
- Elsewhere: RCSB PDB 1XAU · PDBe 1XAU · UniProt Q7TSA3
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