MolNFT v1 · #117605 · protein

Crystal structure of HSV-1 UL21 C-terminal domain

5ED7 · Tegument protein UL21: “Crystal structure of HSV-1 UL21 C-terminal domain”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.33). MolNFT v1 #117605 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5ED7
Type: protein
Length: 252 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tegument protein UL21
UniProt: P10205
Ligands: CL
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tegument protein UL21	protein	252	65% helix, 2% strand	P10205

Ligands and binding sites

CL · Chloride ion · ion · 6 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.33	0.77	12	empty

Compared structures

5ED7 · Crystal Structure of HSV-1 UL21 C-terminal Domain · 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 P10205
Elsewhere: RCSB PDB 5ED7 · PDBe 5ED7 · UniProt P10205

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