Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 1262 |
| PDBID: | 5DHY |
| Chains: | AB_C |
| Organism: | Oryctolagus cuniculus, Human immunodeficiency virus 1 |
| Method: | XRD |
| Resolution (Å): | 3.10 |
| Reference: | 10.1016/j.str.2016.04.015 |
| Antibody | |
| Antibody: | Anti-Rev Fv |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | HIV-1 Protein Rev |
| Antigen mutation: | No |
| Durg Target: | |
Sequence information
Antibody
Heavy Chain: A
Mutation: NULL
| >5DHY_A|Chain A, D[auth H]|Anti-Rev Antibody Fab single-chain variable fragment, heavy chain|Oryctolagus cuniculus (9986) QEQLVESGGRLVTPGTALTLTCKVSGFSLSGFWLNWVRQAPGKGLEWVGAIYRGSGSEWYASWAKGRFTISDTSTTVTLKLTSPTTEDTATYFCAADTTDNGYFTIWGPGTLVTVSS |
Light Chain: B
Mutation: NULL
| >5DHY_B|Chain B, E[auth L]|Anti-Rev Antibody Fab single-chain variable fragment, light chain|Oryctolagus cuniculus (9986) ELVMTQTPSSVSEPVGGTVTIKCQASQSISSWLSWYQQKPGQPPKLLIYDASNLASGVPSRFMGSGSGTEYTLTISGVQREDAATYYCLGGYPAASYRTAFGGGTELEII |
Antigen
Chain: C
Mutation: NULL
| >5DHY_C|Chain C, F[auth M]|Protein Rev|Human immunodeficiency virus 1 (11676) MAGRSGDSDEDLLKAVRLIKFLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISERILSTYLG |
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: GLY31 TRP33 TYR52 GLY54 SER55 SER57 GLU58 TRP59 TYR60 LYS65 THR99 ASP100 ASN101 B: SER30 SER31 TRP32 TYR92 ALA94 ALA95 SER96 TYR97 ARG98 C: ASP7 ASP11 LYS14 ALA15 LEU18 PHE21 LEU22 ARG48 GLN51 ILE55 ARG58 ILE59 THR62 TYR63 |
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)
