Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 7320 |
| PDBID: | 7PA5 |
| Chains: | B_A |
| Organism: | Escherichia coli, Camelidae |
| Method: | XRD |
| Resolution (Å): | 3.18 |
| Reference: | 10.1128/aac.01499-22 |
| Antibody | |
| Antibody: | cAbCMY-2(254) VHH |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | CMY-2 β-lactamase |
| Antigen mutation: | No |
| Durg Target: | P05193 |
Sequence information
Antibody
Chain: B
Mutation: NULL
| >7PA5_B|Chain B|nanobody|Camelidae (9835) QVQLVESGGGMVQPGGSLRLSCAASGFTFSNYDMSWVRRAPGKGPEWVSTINTGGGSTSYADSVKGRFTISRDNAKNTLYLQMNSLKPEDTALYYCTIDRGLHYSDLGEYDYWGQGTQVTVSSHHHHHH |
Antigen
Chain: A
Mutation: NULL
| >7PA5_A|Chain A|Beta-lactamase|Escherichia coli (562) AAKTEQQIADIVNRTITPLMQEQAIPGMAVAVIYQGKPYYFTWGKADIANNHPVTQQTLFELGSVSKTFNGVLGGDAIARGEIKLSDPVTKYWPELTGKQWQGIRLLHLATYTAGGLPLQIPDDVRDKAALLHFYQNWQPQWTPGAKRLYANSSIGLFGALAVKPSGMSYEEAMTRRVLQPLKLAHTWITVPQNEQKDYAWGYREGKPVHVSPGQLDAEAYGVKSSVIDMARWVQANMDASHVQEKTLQQGIALAQSRYWRIGDMYQGLGWEMLNWPLKADSIINGSDSKVALAALPAVEVNPPAPAVKASWVHKTGSTGGFGSYVAFVPEKNLGIVMLANKSYPNPVRVEAAWRILEKLQ |
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: GLN1 VAL2 GLN3 LEU4 GLY26 PHE27 THR28 TYR32 ASP33 CYS96 THR97 ILE98 ASP99 ARG100 GLY101 LEU102 HIS103 SER105 ASP106 LEU107 TYR110 ASP111 TYR112 TRP113 GLY114 A: GLY116 PRO118 LEU119 GLN120 PRO122 ASP123 TRP138 GLN139 GLN141 TRP142 LYS147 LEU149 TYR150 ASN152 ARG204 ASN285 GLY286 ASP288 SER289 LYS290 VAL291 LEU293 ALA294 ALA295 LEU296 PRO297 PRO345 PRO347 VAL348 |
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)
