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Human cytomegalovirus protease mutant (C84A, C87A, C138A, C202A) in complex with inhibitor

Analyse Human cytomegalovirus protease mutant (C84A, C87A, C138A, C202A) in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7TCZ
Type: protein
Length: 213 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Assemblin
EC: 3.4.21.97
UniProt: A0A126N917
Ligands: GIT
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Assemblin (EC 3.4.21.97)	protein	213	35% helix, 23% strand	A0A126N917

Ligands and binding sites

GIT · [1-(2-oxopropyl)-4-phenyl-1H-1,2,3-triazol-5-yl]methyl benzylcarbamate · ligand · 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	155	0.44	0.75	23	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

7TCZ · Human cytomegalovirus protease mutant (C84A, C87A, C138A, C202A) in complex with inhibitor · 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 A0A126N917
Elsewhere: RCSB PDB 7TCZ · PDBe 7TCZ · UniProt A0A126N917

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