MolNFT v1 · #101687 · protein

The emcv 3DPOL structure with altered motif a conformation at 2.15A resolution

4NYZ · Genome polyprotein: “The emcv 3DPOL structure with altered motif a conformation at 2.15A resolution”. X-ray diffraction, 2 ligands (GLN, MG), 2 pockets (best druggability 0.75). MolNFT v1 #101687 on GenesisL1: 3D structure, binding…

PDB: 4NYZ
Type: protein
Length: 460 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Genome polyprotein
EC: 3.6.1.15, 3.4.22.28, 2.7.7.48
UniProt: P12296
Ligands: GLN, MG
Pockets: 2 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Genome polyprotein (EC 3.6.1.15, 3.4.22.28, 2.7.7.48)	protein	460	41% helix, 15% strand	P12296

Ligands and binding sites

GLN · Glutamine · ligand · chains A
MG · Magnesium ion · metal · chains A
GOL · Glycerol · additive · chains A

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

Pockets

2 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	943	0.75	0.78	71	GLN, GOL
2	166	0.47	0.76	26	empty

Compared structures

4NYZ · The EMCV 3Dpol structure with altered motif A conformation at 2.15A resolution · 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 P12296
Elsewhere: RCSB PDB 4NYZ · PDBe 4NYZ · UniProt P12296

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