Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 1014 |
| PDBID: | 4W6W |
| Chains: | B_A |
| Organism: | Escherichia coli, Lama glama |
| Method: | XRD |
| Resolution (Å): | 2.51 |
| Reference: | 10.1371/journal.pone.0114691 |
| Antibody | |
| Antibody: | NbFedF6 Nanobody |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | F18 fimbrial adhesin AC |
| Antigen mutation: | No |
| Durg Target: | |
Sequence information
Antibody
Chain: B
Mutation: NULL
| >4W6W_B|Chain B|NbFedF6|Lama glama (9844) QVQLQESGGGSVQAGGSLRLSCAASGYTSGRDSMGWFRQAPGKEREGVACIDTSGIVNYADSVKGRFTISQDSAKKTLYLEMNSLKPEDTALYSCATGPFVYGRGCLGQAFYSYWGQGTQVTVSSHHHHHH |
Antigen
Chain: A
Mutation: NULL
| >4W6W_A|Chain A|F18 fimbrial adhesin AC|Escherichia coli (562) NSSASSAQVTGTLLGTGKTNTTQMPALYTWQHQIYNVNFIPSSSGTLTCQAGTILVWKNGRETQYALECRVSIHHSSGSINESQWGQQSQVGFGTACGNKKCRFTGFEISLRIPPNAQTYPLSSGDLKGSFSLTNKEVNWSASIYVPAIAK |
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: ARG819 ILE851 GLY855 ILE856 VAL857 ASN858 TYR859 ASP861 LYS864 GLY865 ARG866 THR868 ILE869 SER870 GLN871 ASP872 SER873 ALA874 LYS875 TYR879 GLU881 ASN883 GLY903 ARG904 A: GLN64 THR67 LEU69 LYS72 ASN73 ARG75 GLU76 THR77 GLN78 TYR79 ALA80 GLU82 GLN98 TRP99 GLN101 GLN102 GLN104 ASN130 ALA131 TYR134 |
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)
