Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 2159 |
| PDBID: | 6DID |
| Chains: | DC_F |
| Organism: | Human immunodeficiency virus 1, Oryctolagus cuniculus |
| Method: | EM |
| Resolution (Å): | 4.71 |
| Reference: | 10.1016/j.immuni.2018.07.009 |
| Antibody | |
| Antibody: | 10A Fab |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | HIV BG505 SOSIP gp160 |
| Antigen mutation: | No |
| Durg Target: | |
Sequence information
Antibody
Heavy Chain: D
Mutation: NULL
| >6DID_D|Chain H[auth D], J[auth K], L|Monoclonal antibody 10A heavy chain|Oryctolagus cuniculus (9986) QLVESGGGLVQPGASLTLTCTASGFSFSSDYYMCWVRQAPGKGLEWIACIWTANSISYYARWAKGRFTISKTSSTTVTLQMTSLTAADTATYFCARGGSGDGQSLWGPGTLVTVSSGQPKAPSVFPLAPCCGDTPSSTVTLGCLVKGYLPEPVTVTWNSGTLTNGVRTFPSVRQSSGLYSLSSVVSVTSSSQPVTCNVAHPATNTKVDKTVAPS |
Light Chain: C
Mutation: NULL
| >6DID_C|Chain G[auth C], I[auth E], K[auth H]|Monoclonal antibody 10A light chain|Oryctolagus cuniculus (9986) DIVMTQTPASVEAAVGGTVAIKCQASQSIRSYLAWYQQKPGQPPKLLIYEASKLASGVPSRFSGSGSGTQFTLTISGVECDDAATYYCQRNYDSYSGAYYPNGFGGGTEVVVKGDPVAPSVLIFPPAADQVATGTVTIVCVANKYFPDVTVTWEVDGTTQTTGIENSKTPQNSADCTYNLSSTLTLTSTQYNSHKEYTCKVTQGTTSVVQSFNRGDC |
Antigen
Chain: F
Mutation: NULL
| >6DID_F|Chain A, C[auth F], E[auth G]|Envelope glycoprotein gp160|Human immunodeficiency virus 1 (11676) AENLWVTVYYGVPVWKDAETTLFCASDAKAYETEKHNVWATHACVPTDPNPQEIHLENVTEEFNMWKNNMVEQMHTDIISLWDQSLKPCVKLTPLCVTLQCTNVTNNITDDMRGELKNCSFNMTTELRDKKQKVYSLFYRLDVVQINENQGNRSNNSNKEYRLINCNTSAITQACPKVSFEPIPIHYCAPAGFAILKCKDKKFNGTGPCPSVSTVQCTHGIKPVVSTQLLLNGSLAEEEVMIRSENITNNAKNILVQFNTPVQINCTRPNNNTRKSIRIGPGQAFYATGDIIGDIRQAHCNVSKATWNETLGKVVKQLRKHFGNNTIIRFANSSGGDLEVTTHSFNCGGEFFYCNTSGLFNSTWISNTSVQGSNSTGSNDSITLPCRIKQIINMWQRIGQAMYAPPIQGVIRCVSNITGLILTRDGGSTNSTTETFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTRCKRRVVGRRRRRR |
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)
| C: ASP21 ILE22 SER46 GLN47 SER48 ARG50 TYR112 SER114 TYR115 SER116 GLY117 ALA118 TYR119 D: SER48 SER49 ASP50 TYR52 TRP71 ALA73 ASN74 ILE76 TYR78 SER119 F: HIS85 GLU87 ASN88 VAL89 THR90 LYS229 ASP230 LYS231 LYS232 PRO240 SER241 ALA266 GLU267 GLU268 GLU269 ASN289 THR290 LYS344 LYS347 GLN348 |
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)
