Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 777 |
| PDBID: | 4K2U |
| Chains: | IM_B |
| Organism: | Plasmodium falciparum 3D7, Mus musculus |
| Method: | XRD |
| Resolution (Å): | 2.45 |
| Reference: | 10.1371/journal.ppat.1003390 |
| Antibody | |
| Antibody: | R218 Fab |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | malaria. P. falciparum EBA-175 (PfEBA-175) |
| Antigen mutation: | No |
| Durg Target: | |
Sequence information
Antibody
Heavy Chain: I
Mutation: NULL
| >4K2U_I|Chain C[auth H], D[auth I]|Antibody Heavy Chain|Mus musculus (10090) EVQLQQSGAELVKPGASVKLSCTASGFNIKDNYMHWVKQRPEQGLEWIGRIDPANGNTKYDPKFQGKATITADTSSNTAYLQLSSLTSEDTAVYYCARHYDGYFLYYFEYWGQGTTLTVSSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPRDCGCKPCICTVP |
Light Chain: M
Mutation: NULL
| >4K2U_M|Chain E[auth L], F[auth M]|Antibody Light Chain|Mus musculus (10090) LSLDMMSSAQFLGLLLLCFQGTRCDIQMTQTTSSLSASLGDRVTITCRAGQDISNYLNWYQQKPDGTVKLLIYYTSRLHSGVPSRFSGSGSGTDYSLTISNLEQEDIATYFCQQGSTFPWTFGGGTKLEIKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKKGEFQHTGGRY |
Antigen
Chain: B
Mutation: NULL
| >4K2U_B|Chain A, B|Erythrocyte binding antigen 175|Plasmodium falciparum (36329) GRNTSSNNEVLSNCREKRKGMKWDCKKKNDRSNYVCIPDRRIQLCIVNLSIIKTYTKETMKDHFIEASKKESQLLLKKNDNKYNSKFCNDLKNSFLDYGHLAMGNDMDFGGYSTKAENKIQEVFKGAHGEISEHKIKNFRKKWWNEFREKLWEAMLSEHKNNINNCKNIPQEELQITQWIKEWHGEFLLERDNRSKLPKSKCKNNTLYEACEKECIDPCMKYRDWIIRSKFEWHTLSKEYETQKVPKENAENYLIKISENKNDAKVSLLLNNCDAEYSKYCDCKHTTTLVKSVLNGN |
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)
| I: ASP31 ASN32 TYR33 ARG50 ASN54 ASN56 LYS58 TYR96 ASP97 GLY98 TYR99 M: SER30 TYR32 TYR50 ARG53 GLY91 SER92 THR93 PHE94 TRP96 B: GLU149 TRP152 GLU153 LEU156 SER157 LYS160 ASN161 ASN162 ILE163 ASN164 LYS167 ASN168 ILE169 |
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)
