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Crystal structure of the catalytic site mutant (H157Q) of the human cytomegalovirus protease

Analyse Crystal structure of the catalytic site mutant (H157Q) of the human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ID4
Type: protein
Length: 427 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein P40: assemblin protease
EC: 3.4.21.97
UniProt: P16753
Pockets: 7 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protein P40: assemblin protease (EC 3.4.21.97)	protein	208	35% helix, 25% strand	P16753
B	Capsid protein P40: assemblin protease (EC 3.4.21.97)	protein	219	38% helix, 23% strand	P16753

Pockets

7 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	192	0.54	0.78	44	empty
2	61	0.45	0.83	15	empty
3	102	0.40	0.77	20	empty
4	52	0.39	0.81	16	empty
5	60	0.39	0.80	18	empty

Interfaces

1 interface between chains.

A–B · 1603 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

1ID4 · Crystal structure of the catalytic site mutant (H157Q) of the human cytomegalovirus… · 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 P16753
Elsewhere: RCSB PDB 1ID4 · PDBe 1ID4 · UniProt P16753

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