MolNFT v1 · #141090 · protein

Crystal structure of full length NS3 protein (ED4NS2BNS3) from DENV4 in closed conformation

5YVW · Genome polyprotein: “Crystal structure of full length NS3 protein (ED4NS2BNS3) from DENV4 in closed conformation”. X-ray diffraction, 9 pockets (best druggability 0.81). MolNFT v1 #141090 on GenesisL1: 3D structure, binding sites…

PDB: 5YVW
Type: protein
Length: 621 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Genome polyprotein
UniProt: F8TEL4
Pockets: 9 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Genome polyprotein	protein	591	25% helix, 20% strand	F8TEL4
A	Genome polyprotein	protein	30	0% helix, 27% strand	F8TEL4

Ligands and binding sites

EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains B

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

Pockets

9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1123	0.81	0.82	87	empty
2	639	0.67	0.77	74	EPE
3	64	0.44	0.82	26	empty
4	73	0.43	0.81	16	empty
5	62	0.40	0.80	18	empty

Interfaces

1 interface between chains.

B–A · 1237 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

5YVW · Crystal structure of full length NS3 protein (eD4NS2BNS3) from DENV4 in closed… · 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 F8TEL4
Elsewhere: RCSB PDB 5YVW · PDBe 5YVW · UniProt F8TEL4

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