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Crystal structure of vegetative insecticidal PROTEIN2 (VIP2)

Analyse Crystal structure of vegetative insecticidal PROTEIN2 (VIP2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QS1
Type: protein
Length: 1,608 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ADP-ribosyltransferase
EC: 2.4.2.30
Pockets: 20 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	ADP-ribosyltransferase (EC 2.4.2.30)	protein	402	34% helix, 29% strand	—

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1153	0.78	0.80	86	empty
2	197	0.66	0.85	28	empty
3	204	0.66	0.85	29	empty
4	230	0.66	0.84	32	empty
5	287	0.65	0.82	39	empty

Interfaces

5 interfaces between chains.

B–C · 483 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 438 Å² buried · 7 hydrogen bonds · protein-protein
B–D · 435 Å² buried · 4 hydrogen bonds · protein-protein
C–D · 52 Å² buried · 0 hydrogen bonds · protein-protein
A–B · 43 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1QS1 · Crystal structure of vegetative insecticidal PROTEIN2 (VIP2) · 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
Elsewhere: RCSB PDB 1QS1 · PDBe 1QS1

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