Research workbench
Crystal structure of murine CEACAM1B
Analyse Crystal structure of murine CEACAM1B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VST
- Type
- protein
- Length
- 199 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Biliary glycoprotein
- UniProt
- Q61354
- Ligands
- NAG
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biliary glycoprotein | protein | 199 | 3% helix, 52% strand | Q61354 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 5VST · Crystal structure of murine CEACAM1b · 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 Q61354
- Elsewhere: RCSB PDB 5VST · PDBe 5VST · UniProt Q61354
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