Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 763 |
| PDBID: | 4I1N |
| Chains: | B_A |
| Organism: | Escherichia coli K-12, Lama glama |
| Method: | XRD |
| Resolution (Å): | 1.89 |
| Reference: | Not available or To be published |
| Antibody | |
| Antibody: | ca1697 Nanobody |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | Dihydrofolate reductase |
| Antigen mutation: | No |
| Durg Target: | P0ABQ4 |
Sequence information
Antibody
Chain: B
Mutation: NULL
| >4I1N_B|Chain B|Protein ca1697 (nanobody)|lama glama (9844) QVQLQESGGGLVQAGASLRLSCAASERLTVDYAIGWFRQAPGKEREFVAAISWGGGLTVYGESVEGRFTISRDIAKNTMNLQMNVLRPEDTANYYCAASRISYAVWNTIPYNKLTLWGRGTQVTVSSHHHHHH |
Antigen
Chain: A
Mutation: NULL
| >4I1N_A|Chain A|Dihydrofolate reductase|Escherichia coli (83333) MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR |
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)
| B: VAL30 ASP31 TYR32 ALA33 SER52 GLY54 GLY55 LEU57 ARG100 ILE101 SER102 TYR103 ALA104 VAL105 THR108 ILE109 PRO110 LYS113 A: MET16 GLU17 ASN18 ALA19 MET20 PRO21 TRP22 ASN23 HIS45 GLU48 SER49 ILE50 GLY51 ARG52 ASP69 ARG71 |
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)
