Details

Structure visualisation

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Entry information

Complex
AACDB_ID:	7046
PDBID:	4UIF
Chains:	GH_A
Organism:	dengue virus type 2, Homo sapiens
Method:	EM
Resolution (Å):	6.50
Reference:	10.1126/science.aaa8651
Antibody
Antibody:	2D22 Fab
Antibody mutation:	No
INN (Clinical Trial):
Antigen
Antigen:	Dengue virus (DENV) type 2 envelope glycoprotein
Antigen mutation:	No
Durg Target:	P27914; P12823;

Sequence information

Antibody

Heavy Chain: G
Mutation: NULL

>4UIF_G|Chain G, I, K|ANTIGEN-BINDING FRAGMENT OF HUMAN ANTIBODY 2D22 - HEAVY CHAIN|HOMO SAPIENS (9606)
EVQLVESGAEVKKPGSSVKVSCKASGGTFNNYAISWVRQAPGQGLEWMGGIIPIFGGANYAQKFQGRVTITADRSTSTVYMELSGLRSEDTAVYYCARRPQSIFDWNFDLWGRGTLVTVSSAGTKGPS

Light Chain: H
Mutation: NULL

>4UIF_H|Chain H, J, L|ANTIGEN-BINDING FRAGMENT OF HUMAN ANTIBODY 2D22 - LIGHT CHAIN|HOMO SAPIENS (9606)
QSVLTQPPSASGTPGQRVTISCSGSSSNVGSNYVYWYQQLPGTAPKLLIYRNNRRPSGVPDRFSGSKSGTSASLAISGLRSEDEADYYCATWDDSLSGLVFGGGTKLTVLGQPKA

Antigen

Chain: A
Mutation: NULL

>4UIF_A|Chain A, C, E|DENGUE VIRUS SEROTYPE 2 STRAIN PVP94 07 - ENVELOPE PROTEIN|DENGUE VIRUS 2 (11060)
MRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKHPATLRKYCVEAKLTNTTTASRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFTCKKNMEGKVVQPENLEYTIVITPHSGEENAVGNDTGKHGKEIKVTPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQMENKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLSWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVFGAIYGAAFSGVSWTMKILIGVVITWIGMNSRSTSLSVSLVLVGVVTLYLGVMVQA

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: PRO56

A: ASN153

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)

Within the threshold, the structure has no interacting amino acids and cannot be displayed. This may be due to the following reasons:
1. The method used to determine the structure is electron microscopy or nuclear magnetic resonance, which results in too low resolution;
2. the coordinates of some amino acids involved in the interaction in the structure were not detected due to technical limitations. The results are less based on atomic coordinates, but the antibody does target the antigen.

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