Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 122 |
| PDBID: | 1OAZ |
| Chains: | JN_B |
| Organism: | Escherichia coli, Mus musculus |
| Method: | XRD |
| Resolution (Å): | 2.78 |
| Reference: | 10.1126/science.1079731 |
| Antibody | |
| Antibody: | SPE7 Fv |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | THIOREDOXIN 1 |
| Antigen mutation: | No |
| Durg Target: | |
Sequence information
Antibody
Heavy Chain: J
Mutation: NULL
| >1OAZ_J|Chain C[auth H], D[auth J]|IMMUNOGLOBULIN E|MUS MUSCULUS (10090) EVQLQQSGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNGGGTKYNEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCARMWYYGTYYFDYWGQGTTLTVSSAA |
Light Chain: N
Mutation: NULL
| >1OAZ_N|Chain E[auth L], F[auth N]|IMMUNOGLOBULIN E|MUS MUSCULUS (10090) QAVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIGGTNNRAPGVPARFSGSLIGNKAALTITGAQTEDEAIYFCALWYSNHLVFGGGTKLTVLT |
Antigen
Chain: B
Mutation: NULL
| >1OAZ_B|Chain A, B|THIOREDOXIN 1|ESCHERICHIA COLI (562) MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPIEESDDRRYDLVGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLA |
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)
| J: GLU1 VAL2 GLY26 TYR27 THR28 THR30 SER31 TYR32 TRP33 ASP52 ASN54 LYS74 ARG98 TRP100 TYR101 TYR102 GLY103 THR104 TYR105 TYR106 N: THR31 SER32 TYR34 ASN54 ASN55 ARG56 ALA57 PRO58 ASN96 B: CYS32 GLY33 PRO34 ILE35 GLU37 SER38 ARG41 ARG42 TYR43 LEU45 VAL46 GLY47 PRO48 GLY85 ARG87 GLY88 ILE89 PRO90 VAL105 GLY106 ALA107 LEU108 SER109 GLN112 |
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)
