Arsenic in PDB 1jq6: Human Cytomegalovirus Protease Dimer-Interface Mutant, S225Y

All present enzymatic activity of Human Cytomegalovirus Protease Dimer-Interface Mutant, S225Y:
3.4.21.97;

The structure of Human Cytomegalovirus Protease Dimer-Interface Mutant, S225Y, PDB code: 1jq6 was solved by R.Batra, R.Khayat, L.Tong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.30 / 2.30
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	42.270, 108.300, 108.500, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 28.6

The binding sites of Arsenic atom in the Human Cytomegalovirus Protease Dimer-Interface Mutant, S225Y (pdb code 1jq6). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 3 binding sites of Arsenic where determined in the Human Cytomegalovirus Protease Dimer-Interface Mutant, S225Y, PDB code: 1jq6:
Jump to Arsenic binding site number: 1; 2; 3;

Arsenic binding site 1 out of 3 in the Human Cytomegalovirus Protease Dimer-Interface Mutant, S225Y


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Human Cytomegalovirus Protease Dimer-Interface Mutant, S225Y within 5.0Å range: probe atom residue distance (Å) B Occ A:As87 b:58.0 occ:1.00 AS A:CAS87 0.0 58.0 1.0 SG A:CAS87 2.3 49.2 1.0 CB A:CAS87 3.3 34.8 1.0 CB A:CAS202 3.9 40.6 1.0 SG A:CAS202 4.0 43.0 1.0 CE2 A:TYR15 4.4 29.6 1.0 CA A:CAS87 4.7 31.9 1.0 CB A:ALA73 4.8 32.8 1.0 OH A:TYR15 4.9 33.7 1.0

Arsenic binding site 2 out of 3 in the Human Cytomegalovirus Protease Dimer-Interface Mutant, S225Y


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Human Cytomegalovirus Protease Dimer-Interface Mutant, S225Y within 5.0Å range: probe atom residue distance (Å) B Occ A:As161 b:58.5 occ:1.00 AS A:CAS161 0.0 58.5 1.0 SG A:CAS161 2.2 52.0 1.0 CB A:CAS161 3.3 43.5 1.0 OD1 A:ASN62 3.7 34.3 1.0 CD2 A:HIS63 3.8 36.8 1.0 CA A:CAS161 3.9 37.9 1.0 NE2 A:HIS63 4.0 37.2 1.0 CB A:SER132 4.3 45.7 1.0 CA A:ASN62 4.3 32.7 1.0 OG A:SER132 4.5 49.1 1.0 CG A:ASN62 4.5 32.5 1.0 CB A:ASN62 4.7 32.1 1.0 C A:CAS161 4.8 38.2 1.0 N A:SER162 4.8 37.9 1.0 O A:HOH274 4.9 52.1 1.0 N A:CAS161 4.9 35.2 1.0 C A:ASN62 4.9 33.8 1.0 O A:VAL163 4.9 52.0 1.0

Arsenic binding site 3 out of 3 in the Human Cytomegalovirus Protease Dimer-Interface Mutant, S225Y


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of Human Cytomegalovirus Protease Dimer-Interface Mutant, S225Y within 5.0Å range: probe atom residue distance (Å) B Occ A:As202 b:57.0 occ:1.00 AS A:CAS202 0.0 57.0 1.0 SG A:CAS202 2.2 43.0 1.0 O A:HOH271 2.9 47.0 1.0 CB A:CAS202 3.3 40.6 1.0 CA A:CAS202 3.6 36.4 1.0 CG2 A:THR205 4.0 33.9 1.0 CB A:THR205 4.1 35.8 1.0 CG1 A:VAL207 4.1 55.0 1.0 N A:CAS202 4.2 35.8 1.0 OG1 A:THR205 4.4 31.1 1.0 O A:VAL72 4.8 31.3 1.0 C A:CAS202 4.8 35.0 1.0 CA A:ALA73 4.9 33.0 1.0

R.Batra, R.Khayat, L.Tong. Molecular Mechanism For Dimerization to Regulate the Catalytic Activity of Human Cytomegalovirus Protease. Nat.Struct.Biol. V. 8 810 2001.
ISSN: ISSN 1072-8368
PubMed: 11524687
DOI: 10.1038/NSB0901-810