Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 827 |
| PDBID: | 4M62 |
| Chains: | IM_T |
| Organism: | Homo sapiens, synthetic construct |
| Method: | XRD |
| Resolution (Å): | 1.80 |
| Reference: | 10.1371/journal.ppat.1004403 |
| Antibody | |
| Antibody: | GEP2 Fv |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | engineered 4E10 epitope-scaffolds immunogens T117 |
| Antigen mutation: | No |
| Durg Target: | |
Sequence information
Antibody
Heavy Chain: I
Mutation: NULL
| >4M62_I|Chain B[auth H], D[auth I]|GEP2 FV heavy chain|Homo sapiens (9606) QVQLVQSGAEVKKPGSSVKVSCKASGGTFSSYAISWVRQAPGQGLEWMGGIIPIFGTANYAQKFQGRVTITADKSTSTAYMELSSLRSEDTAVYYCAREGTTGSGWLGKPIGAFAYWGQGTLVTVSS |
Light Chain: M
Mutation: NULL
| >4M62_M|Chain A[auth L], C[auth M]|GEP2 FV light chain|Homo sapiens (9606) EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGIPDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPSTFGQGTKVEIKRLVPR |
Antigen
Chain: T
Mutation: NULL
| >4M62_T|Chain E[auth S], F[auth T]|T117|synthetic construct (32630) NAMQGIHFRRHYVRHLPKEVSQNDIIKALASPLINDGMVVSDFADHVITREQNFPTGLPVEPVGVAIPHTDSKYVRQNAISVGILAEPVNFEDAGGEPDPVPVRVVFMLALGNWFDITNVLWWIMDVIQDEDFMQQLLVMNDDEIYQSIYTRISE |
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)
| M: TYR32 TYR91 GLY92 SER93 SER94 SER96 I: SER31 TYR32 ALA33 SER35 TRP47 GLY50 ILE51 ILE53 PHE54 GLY55 THR56 ASN58 GLN61 LYS73 GLU95 PHE100 T: ASN7 ALA8 GLN10 ARG56 PHE60 PRO61 THR62 LEU64 ILE73 HIS75 ASP77 SER78 LYS79 ALA100 GLY101 GLU103 LEU115 GLY118 ASN119 TRP120 PHE121 ASP122 ILE123 THR124 ASN125 LEU127 TRP128 MET131 |
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)
