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Crystal structure of the broadly neutralizing influenza a antibody vrc 315 13-1B02 Fab.

Analyse Crystal structure of the broadly neutralizing influenza a antibody vrc 315… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TY6
Type: protein
Length: 436 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vrc 315 13-1B02 Fab heavy chain; Vrc 315 13-1B02 Fab light chain
Pockets: 3 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	Vrc 315 13-1B02 Fab heavy chain	protein	224	9% helix, 48% strand	—
L	Vrc 315 13-1B02 Fab light chain	protein	212	5% helix, 51% strand	—

Ligands and binding sites

GOL · Glycerol · additive · 3 copies · chains H, L

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	259	0.51	0.75	36	empty
2	51	0.49	0.87	21	GOL
3	90	0.32	0.73	26	GOL

Interfaces

1 interface between chains.

H–L · 1952 Å² buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

5TY6 · Crystal structure of the broadly neutralizing Influenza A antibody VRC 315 13-1b02 Fab. · the same entry in another collection · chain H against H, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 5TY6 · PDBe 5TY6

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