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PRRSV NSP4

Analyse PRRSV NSP4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5Y4L
Type: protein
Length: 800 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-structural protein
UniProt: A1E8J1
Pockets: 12 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Non-structural protein	protein	203	8% helix, 44% strand	A1E8J1
A, C, D	Non-structural protein	protein	199	8% helix, 45% strand	A1E8J1

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	136	0.67	0.89	29	empty
2	124	0.66	0.89	26	empty
3	333	0.58	0.77	43	empty
4	277	0.56	0.77	56	empty
5	91	0.48	0.82	19	empty

Interfaces

4 interfaces between chains.

B–C · 1070 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 1048 Å² buried · 6 hydrogen bonds · protein-protein
B–D · 444 Å² buried · 2 hydrogen bonds · protein-protein
B–A · 222 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5Y4L · PRRSV nsp4 · the same entry in another collection · chain B against B, 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 A1E8J1
Elsewhere: RCSB PDB 5Y4L · PDBe 5Y4L · UniProt A1E8J1

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