Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 263 |
| PDBID: | 2H8P |
| Chains: | AB_C |
| Organism: | Mus musculus, synthetic construct |
| Method: | XRD |
| Resolution (Å): | 2.25 |
| Reference: | 10.1021/ja0631955 |
| Antibody | |
| Antibody: | 2H8P Fab |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | KcsA Channel |
| Antigen mutation: | No |
| Durg Target: | P0A333; P0A334; |
Sequence information
Antibody
Heavy Chain: A
Mutation: NULL
| >2H8P_A|Chain A|FAB heavy chain|Mus musculus (10090) QVQLQQPGAELVKPGASVKLSCKASGYTFTSDWIHWVKQRPGHGLEWIGEIIPSYGRANYNEKIQKKATLTADKSSSTAFMQLSSLTSEDSAVYYCARERGDGYFAVWGAGTTVTVSSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSSWPSETVTCNVAHPASSTKVDKKIVPRD |
Light Chain: B
Mutation: NULL
| >2H8P_B|Chain B|FAB light chain|Mus musculus (10090) DILLTQSPAILSVSPGERVSFSCRASQSIGTDIHWYQQRTNGSPRLLIKYASESISGIPSRFSGSGSGTDFTLSINSVESEDIANYYCQQSNRWPFTFGSGTKLEIKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRN |
Antigen
Chain: C
Mutation: NULL
| >2H8P_C|Chain C|KcsA Channel|synthetic construct (32630) SALHWRAAGAATVLLVIVLLAGSYLAVLAERGAPGAQLITYPRALWWACETATTVGYXDLYPVTLWGRLVAVVVMVAGITSFGLVTAALATWFVGREQERR |
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: THR30 SER31 TRP33 GLU50 ILE52 SER54 TYR55 ARG57 ASN59 GLU62 GLU99 ARG100 GLY101 ASP102 GLY103 B: ASP1 SER28 ASP32 TYR50 SER91 ASN92 ARG93 TRP94 PRO95 PHE96 C: TYR45 LEU46 VAL48 LEU49 ALA50 ARG52 GLY53 ALA54 PRO55 GLY56 ALA57 GLN58 ILE60 THR61 TYR62 PRO63 ARG64 TRP87 |
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)
