Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 557 |
| PDBID: | 3K74 |
| Chains: | B_A |
| Organism: | Escherichia coli K-12, Lama glama |
| Method: | XRD |
| Resolution (Å): | 1.95 |
| Reference: | 10.1016/j.jmb.2011.01.017 |
| Antibody | |
| Antibody: | 216 Nanobody |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | Dihydrofolate reductase |
| Antigen mutation: | No |
| Durg Target: | P0ABQ4 |
Sequence information
Antibody
Chain: B
Mutation: NULL
| >3K74_B|Chain B|Nanobody|Lama glama (9844) QLQESGGGLVQPGGSLRLSCAASGFTFNNYWMYWVRRAPGKGLEWVSMINPGGIITKYAESVKGRFTISRDNAKNTLYLQMNSLTSEDTAVYYCAKDWATGLAKKGQGTQVTVSS |
Antigen
Chain: A
Mutation: NULL
| >3K74_A|Chain A|Dihydrofolate reductase|Escherichia coli K-12 (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: TRP192 TYR194 GLY203 LEU204 TRP206 MET209 ASN211 PRO212 ILE215 ILE216 THR217 LYS218 TYR219 ALA220 GLU221 LYS224 TRP259 ALA260 THR261 GLY262 A: GLU17 ASN18 ALA19 MET20 PRO21 TRP22 ASN23 ASP116 ALA117 GLU118 VAL119 GLU120 ALA143 ASP144 ALA145 GLN146 SER148 HIS149 |
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)
