Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 6172 |
| PDBID: | 8EZL |
| Chains: | H_A |
| Organism: | Plasmodium falciparum |
| Method: | XRD |
| Resolution (Å): | 2.30 |
| Reference: | 10.1038/s41541-023-00712-z |
| Antibody | |
| Antibody: | AS01-50 scFv |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | Plasmodium falciparum 25 kDa ookinete surface antigen |
| Antigen mutation: | No |
| Durg Target: | |
Sequence information
Antibody
Chain: H
Mutation: NULL
| >8EZL_H|Chain B[auth H]|Transmission-reducing antibody AS01-50, single chain Fv|Homo sapiens (9606) TGQITLKESGPTLVKPTQTLTLTCTFSGSSLSTSGVGVGWIRQPPGKALEWLALIYWNDDKRYSPSLKRRLTITKDTSKNQVVLTMTNMDPVDTATYYCVHRGSAPYYYDSSGYYSTFYYFDYWGQGTLVTVSSGGGGSGGGGSGGGGSGGGGSQPVLTQPPSASASLGASLSLTCTLSSGYNNYKVDWYQQRPGKGPRFVMRVGTGGIVGSKGDGIPDRFSVLGSGLNRNLTIKNIQEDDESDYHCGADHGSGSNLDYVVFGGGTKLTVLGTKHHHHHH |
Antigen
Chain: A
Mutation: NULL
| >8EZL_A|Chain A|25 kDa ookinete surface antigen|Plasmodium falciparum NF54 (5833) TGKVTVDTVCKRGFLIQMSGHLECKCENDLVLVNEETCEEKVLKCDEKTVNKPCGDFSKCIKIDGNPVSYACKCNLGYDMVNNVCIPNECKQVTCGNGKCILDTSNPVKTGVCSCNIGKVPNVQDQNKCSKDGETKCSLKCLKEQETCKAVDGIYKCDCKDGFIIDQESSICTGTKHHHHHH |
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)
| H: SER28 LEU29 SER30 THR31 SER32 SER102 PRO104 TYR105 TYR106 TYR107 ASP108 GLY111 TYR112 TYR113 SER114 THR115 PHE116 TYR117 ASN182 TYR183 LYS184 ARG201 VAL208 ASP248 HIS249 GLY250 SER251 GLY252 SER253 A: GLU45 VAL48 ASN49 LYS57 CYS58 ILE59 LYS60 ILE61 ASP62 GLY63 ASN64 PRO65 VAL66 SER67 LYS71 CYS72 ASN73 LEU74 ASP77 ASN86 LYS89 GLN90 |
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)
