Research workbench
Chimera of mouse cadherin-11 EC1 and mouse cadherin-6 EC2
Analyse Chimera of mouse cadherin-11 EC1 and mouse cadherin-6 EC2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CGB
- Type
- protein
- Length
- 204 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P55288, P97326
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 204 | — | P55288, P97326 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- ACT · Acetate ion · additive
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6CGB · chimera of mouse cadherin-11 EC1 and mouse cadherin-6 EC2 · the same entry in another collection · chain A against A, TM-score 1.00
- P55288 · AlphaFold monomer V2.0 prediction for cadherin-11 (P55288) · a predicted model of the same protein · chain A against A, TM-score 0.96
- P97326 · AlphaFold monomer V2.0 prediction for cadherin-6 (P97326) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P55288
- Every structure of UniProt P97326
- Elsewhere: RCSB PDB 6CGB · PDBe 6CGB · UniProt P55288 · UniProt P97326
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