Research workbench
The bigi domain of beta protein from S. agalactiae bound to CEACAM1
Analyse The bigi domain of beta protein from S. agalactiae bound to CEACAM1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V3P
- Type
- protein
- Length
- 421 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P13688, P27951
- Ligands
- SO4
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 108 | — | P13688 |
| B | — | protein | 107 | — | P13688 |
| C, D | — | protein | 103 | — | P27951 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B, D
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6V3P · The BIgI domain of beta protein from S. agalactiae bound to CEACAM1 · the same entry in another collection · chain D against D, TM-score 1.00
- P13688 · AlphaFold monomer V2.0 prediction for carcinoembryonic antigen- related cell adhesion… · a predicted model of the same protein · chain B against A, TM-score 0.98
- P27951 · AlphaFold monomer V2.0 prediction for IgA Fc receptor (P27951) · a predicted model of the same protein · chain D against A, TM-score 0.96
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 P13688
- Every structure of UniProt P27951
- Elsewhere: RCSB PDB 6V3P · PDBe 6V3P · UniProt P13688 · UniProt P27951
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