MolNFT v1 · #10028 · protein

Crystal structure of the catalytic site mutant (H157A) of the human cytomegalovirus protease

1IEC · Capsid protein P40: assemblin protease: “Crystal structure of the catalytic site mutant (H157A) of the human cytomegalovirus protease”. X-ray diffraction, 5 pockets (best druggability 0.51). MolNFT v1 #10028 on GenesisL1: 3D…

PDB: 1IEC
Type: protein
Length: 426 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: 5 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 37% 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, 25% strand	P16753
B	Capsid protein P40: assemblin protease (EC 3.4.21.97)	protein	219	38% helix, 22% strand	P16753

Pockets

5 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	60	0.51	0.87	15	empty
2	106	0.50	0.81	28	empty
3	55	0.38	0.80	15	empty
4	96	0.37	0.76	19	empty
5	69	0.29	0.73	15	empty

Interfaces

1 interface between chains.

A–B · 1582 Å² buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (nonstandard).

Compared structures

1IEC · Crystal structure of the catalytic site mutant (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 1IEC · PDBe 1IEC · UniProt P16753

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