Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 5184 |
| PDBID: | 7UP9 |
| Chains: | HL_G |
| Organism: | Henipavirus nipahense, Mus musculus |
| Method: | EM |
| Resolution (Å): | 2.90 |
| Reference: | 10.1038/s41467-023-36995-y |
| Antibody | |
| Antibody: | 2D3 Fab |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | Henipavirus nipahense fusion glycoprotein F0 |
| Antigen mutation: | No |
| Durg Target: | |
Sequence information
Antibody
Heavy Chain: H
Mutation: NULL
| >7UP9_H|Chain D[auth H]|Fab 2D3 heavy chain|Mus musculus (10090) MEFGLSWIFLAAILKGVQCQVQLKQSGPGLVAPSQSLSITCTVSGFSLTSYALSWVRQPPGKGLEWLGVIWVGGVTNYNSALKSRLTISKDNSKSQVFLKMNSLQSEDTARYYCASRHLSTGAMDYWGQGTSVTVSA |
Light Chain: L
Mutation: NULL
| >7UP9_L|Chain E[auth L]|Fab 2D3 light chain|Mus musculus (10090) MEFGLSWIFLAAILKGVQCDVLMTQSPLSLPVSLGDQASISCRSSQSIVHSNGDTYFEWYLQKPGQSPKLLIYKVSNRFSGVPNRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSYVPYTFGGGTKLEIK |
Antigen
Chain: G
Mutation: NULL
| >7UP9_G|Chain A, B[auth D], C[auth G]|Fusion glycoprotein F0|Nipah henipavirus (3052225) MVVILDKRCYCNLLILILMISECSVGILHYEKLSKIGLVKGVTRKYKIKSNPLTKDIVIKMIPNVSNMSQCTGSVMENYKTRLNGILTPIKGALEIYKNNTHDCVGDVRLAGVCMAGVAIGIATAAQITAGVALYEAMKNADNINKLKSSIESTNEAVVKLQETAEKTVYVFTALQDYINTNLVPTIDKIPCKQTELSLDLALSKYLSDLLFVFGPNLQDPVSNSMTIQAISQAFGGNYETLLRTLGYATEDFDDLLESDSITGQIIYVDLSSYYIIVRVYFPILTEIQQAYIQELLPVSFNNDNSEWISIVPNFILVRNTLISNIEIGFCLITKRSVICNQDYATPMTNNMRECLTGSTEKCPRELVVSSHVPRFALSNGVLFANCISVTCQCQTTGRAISQSGEQTLLMIDNTTCPTAVLGNVIISLGKYLGSVNYNSEGIAIGPPVFTDKVDISSQISSMNQSLQQSKDYIK |
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: THR30 SER31 TRP52 VAL53 GLY54 VAL56 ASN58 ARG95 LEU97 SER98 L: SER27 ASN28 GLY29 ASP30 TYR32 GLY91 SER92 VAL94 TYR96 G: LYS146 LEU147 SER149 SER150 VAL159 LYS160 LEU161 GLN162 GLU163 THR164 ALA165 GLU166 LYS167 THR168 TYR170 THR245 |
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)
