MolNFT v1 · #113238 · protein

Crystal structure of trichoplusia ni CPV15 polyhedra

5A98 · Polyhedrin: “Crystal structure of trichoplusia ni CPV15 polyhedra”. X-ray diffraction, 2 ligands (ATP, MG), 5 pockets (best druggability 0.42). MolNFT v1 #113238 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5A98
Type: protein
Length: 235 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polyhedrin
UniProt: Q9ELS6
Ligands: ATP, MG
Pockets: 5 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polyhedrin	protein	235	23% helix, 25% strand	Q9ELS6

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A
MG · Magnesium ion · metal · 3 copies · chains A

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

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	140	0.42	0.75	17	empty
2	133	0.38	0.74	23	empty
3	60	0.37	0.79	19	empty
4	94	0.37	0.75	22	empty
5	55	0.26	0.73	19	empty

Compared structures

5A98 · Crystal structure of Trichoplusia ni CPV15 polyhedra · 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 Q9ELS6
Elsewhere: RCSB PDB 5A98 · PDBe 5A98 · UniProt Q9ELS6

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