Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 416 |
| PDBID: | 3AB0 |
| Chains: | BC_A |
| Organism: | Bacillus anthracis str. '34F2 (NMRC), Mus musculus |
| Method: | XRD |
| Resolution (Å): | 3.09 |
| Reference: | 10.1002/prot.22971 |
| Antibody | |
| Antibody: | A4D11 Fv |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | Bacillus anthracis major spore surface protein(BclA) |
| Antigen mutation: | No |
| Durg Target: | |
Sequence information
Antibody
Heavy Chain: B
Mutation: NULL
| >3AB0_B|Chain B, E|antibody ScFv fragment, heavy chain|Mus musculus (10090) EVKLVESGGGLVKPGGSLKLSCSASGFTFSSYAMSWVRQTPEKRLEWVASISTGGDTHYQDSVKGRFTTSRDNARNILTLQMSSLRSEDTAMYYCARNRGWYFDVWGAGTTVTVSSG |
Light Chain: C
Mutation: NULL
| >3AB0_C|Chain C, F|antibody ScFv fragment, light chain|Mus musculus (10090) SQIVLTQSPAIMSASPGEKVTISCSARSSVSYMYWYQQKSGSSPKPWIYRTSNLASGVPARFSGSGSGTSYSLTISSMEAEDAATYYCQQYHSYPPTFGGGTKLEI |
Antigen
Chain: A
Mutation: NULL
| >3AB0_A|Chain A, D|BclA protein|Bacillus anthracis (526966) GLGLPAGLYAFNSGGISLDLGINDPVPFNTVGSKFGTAISQLDADTFVISETGFYKITVIANTATASVLGGLTIQVNGVPVPGTGSSLISLGAPIVIQAITQITTTPSLVEVIVTGLGLSLALGTSASIIIEKVAL |
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: SER31 TYR32 ALA33 SER50 SER52 THR53 GLY54 ASP56 HIS58 ASN98 ARG99 GLY100 TRP101 C: SER31 TYR32 TYR49 ARG50 SER52 ASN53 TYR91 HIS92 SER93 TYR94 A: ILE95 GLY100 ILE101 ASN102 ASP103 PRO104 ASN108 LYS113 SER119 GLN120 LEU121 ASP122 ALA123 ASP124 THR125 VAL127 GLN154 ASN156 GLY157 VAL158 PRO186 LEU188 GLU190 ILE192 |
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)
