Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 5299 |
| PDBID: | 7VYT |
| Chains: | BC_A |
| Organism: | Homo sapiens |
| Method: | XRD |
| Resolution (Å): | 1.53 |
| Reference: | 10.1080/19420862.2021.2013750 |
| Antibody | |
| Antibody: | anti-TIGIT MG1131 Fv |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | T-cell immunoreceptor with Ig and ITIM domains |
| Antigen mutation: | No |
| Durg Target: | |
Sequence information
Antibody
Heavy Chain: B
Mutation: NULL
| >7VYT_B|Chain B, E[auth H]|MG1131 heavy chain variable region|Homo sapiens (9606) MEVQLVQSGAEVKKPGASVKVSCKASGYTFTSYYMHWVRQAPGQGLEWMGIINPSGGSTSYAQKFQGRVTMTRDTSTSTVYMELSSLRSEDTAVYYCASRSGSGWFGALDYWGQGTLVTVSS |
Light Chain: C
Mutation: NULL
| >7VYT_C|Chain D[auth C], F[auth L]|MG1131 light chain variable region|Homo sapiens (9606) GGGGSGGGGSGGGGSGGGGSEIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGIPDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPGGTFGQGTKVEIKRVDKLA |
Antigen
Chain: A
Mutation: NULL
| >7VYT_A|Chain A, C[auth T]|T-cell immunoreceptor with Ig and ITIM domains|Homo sapiens (9606) MTGTIETTGNISAEKGGSIILQCHLSSTTAQVTQVNWEQQDQLLAICNADLGWHISPSFKDRVAPGPGLGLTLQSLTVNDTGEYFCIYHTYPDGTYTGRIFLEVLES |
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: TYR33 ILE50 ASN52 SER57 THR58 SER59 TYR60 GLN62 GLN65 GLY103 TRP104 PHE105 C: GLY-2 GLY-1 SER0 ILE2 GLN27 SER30 SER31 SER32 TYR33 GLY93 SER94 SER95 PRO96 A: GLN53 THR55 GLN56 ASN58 GLU60 GLN61 GLN62 ASP63 GLN64 LEU65 ILE68 ASN70 ASP72 LEU73 GLY74 TRP75 HIS76 ILE109 HIS111 THR112 TYR113 PRO114 ASP115 GLY116 THR117 |
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)
