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Structural characterization of the dual glycan binding adeno- associated virus serotype 6

Analyse Structural characterization of the dual glycan binding adeno- associated virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OAH
Type: protein
Length: 519 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein VP1
UniProt: O56137
Ligands: CYT, OAH
Pockets: 6 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protein VP1	protein	519	7% helix, 34% strand	O56137

Ligands and binding sites

CYT · 6-aminopyrimidin-2(1H)-one · ligand · chains A
OAH · 9-(2-deoxy-5-O-phosphono-alpha-D-threo-pentofuranosyl)-9H-purin-6-amine · ligand · chains A

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

Pockets

6 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	562	0.65	0.76	76	empty
2	113	0.44	0.78	22	OAH
3	154	0.40	0.73	19	empty
4	143	0.39	0.73	21	empty
5	58	0.35	0.78	19	empty

Compared structures

3OAH · Structural Characterization of the Dual Glycan Binding Adeno-Associated Virus Serotype 6 · the same entry in another collection · chain A against A, 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
Every structure of UniProt O56137
Elsewhere: RCSB PDB 3OAH · PDBe 3OAH · UniProt O56137

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