MolNFT v1 · #134800 · protein

Crystal structure of zika virus NS5 protein

5TFR · Genome polyprotein: “Crystal structure of zika virus NS5 protein”. X-ray diffraction, 2 ligands (SAH, ZN), 20 pockets (best druggability 0.80). MolNFT v1 #134800 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5TFR
Type: protein
Length: 1,764 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Genome polyprotein
EC: 3.4.21.91, 3.6.1.15, 3.6.4.13, 2.1.1.56, 2.1.1.57, 2.7.7.48
UniProt: Q32ZE1
Ligands: SAH, ZN
Pockets: 20 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Genome polyprotein (EC 3.4.21.91, 3.6.1.15, 3.6.4.13, 2.1.1.56, 2.1.1.57, 2.7.7.48)	protein	882	43% helix, 14% strand	Q32ZE1

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
ZN · Zinc ion · metal · 4 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	960	0.80	0.82	91	empty
2	854	0.78	0.81	72	empty
3	146	0.64	0.86	24	empty
4	541	0.63	0.75	48	SAH
5	448	0.61	0.76	42	SAH

Interfaces

1 interface between chains.

A–B · 1233 Å² buried · 23 hydrogen bonds · protein-protein

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 Q32ZE1
Elsewhere: RCSB PDB 5TFR · PDBe 5TFR · UniProt Q32ZE1

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