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Crystal structure of the catalytic site mutant S134A/H157A of the human cytomegalovirus protease

Analyse Crystal structure of the catalytic site mutant S134A/H157A 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: 1IEG
Type: protein
Length: 430 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: 6 · best druggability 0.52

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protein P40: assemblin protease (EC 3.4.21.97)	protein	207	36% helix, 23% strand	P16753
B	Capsid protein P40: assemblin protease (EC 3.4.21.97)	protein	223	36% helix, 23% strand	P16753

Pockets

6 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	58	0.52	0.88	16	empty
2	55	0.40	0.81	16	empty
3	105	0.40	0.76	21	empty
4	54	0.37	0.80	14	empty
5	93	0.36	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 1607 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

1IEG · Crystal structure of the catalytic site mutant S134A/H157A 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 1IEG · PDBe 1IEG · UniProt P16753

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