Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 2289 |
| PDBID: | 6I07 |
| Chains: | A_C |
| Organism: | Homo sapiens |
| Method: | XRD |
| Resolution (Å): | 2.35 |
| Reference: | 10.1073/pnas.1819085116 |
| Antibody | |
| Antibody: | MM-131 scFv |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | Epithelial cell adhesion molecule |
| Antigen mutation: | Yes |
| Durg Target: | P16422 |
Sequence information
Antibody
Chain: A
Mutation: NULL
| >6I07_A|Chain A, B|Single chain Fv|Homo sapiens (9606) DIVMTQSPLSLPVTPGEPASISCRSTKSLLHSDGITYLYWYLQKPGQSPQLLIYQLSNLASGVPDRFSSSGSGTDFTLKISRVEAEDEGVYYCAQNLEIPRTFGCGTKLEIKRTGGGGSGGGGSGGGGSGGGGSQVQLVQSGAEVKKPGESVKISCKASGYTFTNYGMNWVRQQPGQCLKWMGWINTYTGESTYADDFKGRFAFSLDTSASTAYLQLSSLRSEDTAVYFCARFAIKGDYWGQGTLVTVSSGGGGGSHHHHHH |
Antigen
Chain: C
Mutation: N51Q/N88Q/N175Q
| >6I07_C|Chain C, D|Epithelial cell adhesion molecule|Homo sapiens (9606) QEECVCENYKLAVNCFVNNNRQCQCTSVGAQNTVICSKLAAKCLVMKAEMQGSKLGRRAKPEGALQNNDGLYDPDCDESGLFKAKQCQGTSMCWCVNTAGVRRTDKDTEITCSERVRTYWIIIELKHKAREKPYDSKSLRTALQKEITTRYQLDPKFITSILYENNVITIDLVQQSSQKTQNDVDIADVAYYFEKDVKGESLFHSKKMDLTVNGEQLDLDPGQTLIYYVDEKAPEFSMQGLKGGGGSHHHHHH |
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)
| A: HIS31 ASP33 TYR37 TYR39 ASN96 LEU97 GLU98 ILE99 ARG101 THR157 ASN158 TYR159 GLY160 ASN162 TRP177 ASN179 THR180 TYR181 THR182 GLU184 ARG225 PHE226 ALA227 ILE228 LYS229 C: GLU25 GLU26 CYS27 VAL28 VAL36 ASN37 CYS38 PHE39 VAL40 ASN41 ASN42 ARG44 THR49 VAL51 GLY52 ALA53 GLN54 GLN74 |
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)
