Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 5951 |
| PDBID: | 8DAM |
| Chains: | B_A |
| Organism: | Mus musculus, Lama glama |
| Method: | XRD |
| Resolution (Å): | 2.00 |
| Reference: | 10.1038/s41467-022-35025-7 |
| Antibody | |
| Antibody: | F3 VHH |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | Mus musculus voltage-dependent L-type calcium channel subunit beta-1 |
| Antigen mutation: | No |
| Durg Target: | Q02641; Q02641; |
Sequence information
Antibody
Chain: B
Mutation: NULL
| >8DAM_B|Chain B|nanobody F3|Lama glama (9844) GQVQLQESGGGLVQAGGSLRLSCVASGRTFSSYAMGWFRQAPGKEREFVAAIDWSGGTASHADSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCAASSYWSRSVDEYDYWGQGTQVTVSS |
Antigen
Chain: A
Mutation: NULL
| >8DAM_A|Chain A|Voltage-dependent L-type calcium channel subunit beta-1|Mus musculus (10090) GSAESYTSRPSDSDVSLEEDREALRKEAERQALAQLEKAKTKPVAFAVRTNVGYNPSPGDEVPVQGVAITFEPKDFLHIKEKYNNDWWIGRLVKEGCEVGFIPSPVKLDSLRLLQEQTLRQNRLSSSKSGDNSSSSLGDVVTGTRRPTPPASAKQKQKSTEHVPPYDVVPSMRPIILVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKHIIIERSNTRSSLAEVQSEIERIFELARTLQLVALDADTINHPAQLSKTSLAPIIVYIKITSPKVLQRLIKSRGKSQSKHLNVQIAASEKLAQCPPEMFDIILDENQLEDACEHLAEYLEAYWKATHPPSSTPPNPLLNRT |
Interaction
1、Solvent accessible surface areas (SASA) were calculated (Naccess V2.1.1) for each residue in antibody and antigen, respectively. The residues with SASA loss in binding of more than 1Å2 were classified as interacting residues.
Interacting residues (ΔSASA based)
| B: THR29 SER31 SER32 TYR33 ASP53 TRP54 SER55 GLY57 THR58 ALA59 SER60 HIS61 LYS66 GLY67 ASN75 ALA76 SER101 TYR102 TRP103 GLU109 ASP111 TYR112 A: ALA102 PHE103 VAL105 ILE136 GLU138 LYS139 ASN142 TRP145 SER161 PRO162 VAL163 ASP166 GLU218 HIS219 VAL220 PRO221 PRO222 TYR223 ASP224 VAL225 ALA300 GLN303 SER304 GLU307 PHE310 SER336 |
2、We defined interacting paratope-epitope residues by a distance cutoff of < 5Å . Two amino acids are considered as interacting residues if they have at least one atom within a distance of 5 Å from any atom.
Interacting residues (Atom distance based)
