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The crystal structure of novel chondroition lyase odv-E66, baculovirus envelope protein

Analyse The crystal structure of novel chondroition lyase odv-E66, baculovirus envelope… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VSM
Type: protein
Length: 633 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Occlusion-derived virus envelope protein E66
UniProt: Q00704
Pockets: 5 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Occlusion-derived virus envelope protein E66	protein	633	29% helix, 27% strand	Q00704

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

5 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	60	0.72	0.98	17	empty
2	104	0.39	0.75	26	empty
3	97	0.38	0.76	21	empty
4	82	0.37	0.76	14	empty
5	51	0.26	0.74	16	empty

Compared structures

3VSM · The crystal structure of novel chondroition lyase ODV-E66, baculovirus envelope protein · 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 Q00704
Elsewhere: RCSB PDB 3VSM · PDBe 3VSM · UniProt Q00704

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