Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 7052 |
| PDBID: | 4WEN |
| Chains: | B_A |
| Organism: | Escherichia coli, Lama glama |
| Method: | XRD |
| Resolution (Å): | 1.89 |
| Reference: | 10.1186/s13567-015-0151-x |
| Antibody | |
| Antibody: | V2 VHH |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | F4 fimbrial adhesin FaeG |
| Antigen mutation: | No |
| Durg Target: | |
Sequence information
Antibody
Chain: B
Mutation: NULL
| >4WEN_B|Chain B|Anti-F4+ETEC bacteria VHH variable region|Lama glama (9844) QVQLQESGGGLVQPGGSLRLSCTASGSISSINAMGWYRQAPGSKREFVAHITNTGVTEFADSVKGRFTISRDNAKTTVDLQMNSLKPEDTAVYYCAATDWGTLLIKGIDHWGKGTQVTVSSHHHHHH |
Antigen
Chain: A
Mutation: NULL
| >4WEN_A|Chain A|K88 fimbrial protein AC|Escherichia coli (562) WMTGHHHHHHDDYRQKWEWKVGTGLNGFGNVLNDLTNGGTKLTITVTGNKPILLGRTKEAFATPVTGGVDGIPHIAFTDYEGASVVLRNPDGETNKKGLAYFVLPMKNAEGTKVGSVKVNASYAGVLGRGGVTSADGELLSLFADGLSSIFYGGLPRGSELSAGSAAAARTKLFGSLSRNDILGQIQRVNANITSLVDVAGSYRENMEYTDGTVVSAAYALGIANGQTIEATFNQAVTTSTQWSAPLNVAITYYDNKQMTGDFNGSVDIGGSITA |
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: ASN832 TYR837 THR854 VAL856 GLU858 ASP861 LYS864 ASP899 TRP900 GLY901 THR902 LEU904 ILE905 LYS906 GLY907 ASP909 A: GLU26 LYS28 VAL29 GLY30 THR31 GLY32 THR55 GLY56 ASN57 LYS58 PRO59 LEU62 ARG64 LYS180 LEU181 PHE182 GLY183 SER184 ASP189 SER274 ASP276 |
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)
