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Chlorine in PDB 3a6k: The E122Q Mutant Creatininase, Mn-Zn Type

Enzymatic activity of The E122Q Mutant Creatininase, Mn-Zn Type

All present enzymatic activity of The E122Q Mutant Creatininase, Mn-Zn Type:
3.5.2.10;

Protein crystallography data

The structure of The E122Q Mutant Creatininase, Mn-Zn Type, PDB code: 3a6k was solved by Y.Nakajima, K.Yamashita, K.Ito, T.Yoshimoto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.20
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 164.200, 164.200, 164.700, 90.00, 90.00, 120.00
R / Rfree (%) 20.7 / 23.7

Other elements in 3a6k:

The structure of The E122Q Mutant Creatininase, Mn-Zn Type also contains other interesting chemical elements:

Manganese (Mn) 6 atoms
Zinc (Zn) 6 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The E122Q Mutant Creatininase, Mn-Zn Type (pdb code 3a6k). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the The E122Q Mutant Creatininase, Mn-Zn Type, PDB code: 3a6k:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in 3a6k

Go back to Chlorine Binding Sites List in 3a6k
Chlorine binding site 1 out of 6 in the The E122Q Mutant Creatininase, Mn-Zn Type


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The E122Q Mutant Creatininase, Mn-Zn Type within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:46.6
occ:1.00
 MN A:MN300 2.7 40.7 1.0
ZN A:ZN301 3.0 37.2 1.0
OD2 A:ASP45 3.7 32.8 1.0
ND1 A:HIS178 3.8 51.0 1.0
OE2 A:GLU183 4.0 44.4 1.0
OD1 A:ASP45 4.0 30.6 1.0
O A:GLY119 4.1 35.9 1.0
CG A:ASP45 4.2 31.2 1.0
N A:TYR121 4.3 40.9 1.0
OE1 A:GLU183 4.3 47.3 1.0
CD A:GLU183 4.4 46.6 1.0
OE1 A:GLU34 4.4 39.2 1.0
ND1 A:HIS120 4.5 37.5 1.0
CE1 A:HIS178 4.5 48.9 1.0
CA A:HIS120 4.6 36.9 1.0
CB A:TYR121 4.7 49.2 1.0
O A:SER78 4.8 65.8 1.0
NE2 A:HIS36 4.8 33.2 1.0
O A:HOH1141 4.9 37.2 1.0
CG A:HIS178 4.9 51.9 1.0
C A:HIS120 5.0 37.8 1.0

Chlorine binding site 2 out of 6 in 3a6k

Go back to Chlorine Binding Sites List in 3a6k
Chlorine binding site 2 out of 6 in the The E122Q Mutant Creatininase, Mn-Zn Type


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The E122Q Mutant Creatininase, Mn-Zn Type within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl302

b:49.6
occ:1.00
 MN B:MN300 2.8 39.6 1.0
ZN B:ZN301 3.1 33.0 1.0
OE1 B:GLU183 3.6 40.9 1.0
ND1 B:HIS178 3.7 45.0 1.0
OD2 B:ASP45 4.0 27.2 1.0
OD1 B:ASP45 4.1 23.9 1.0
CD B:GLU183 4.2 39.4 1.0
OE2 B:GLU183 4.2 39.4 1.0
O B:GLY119 4.2 40.1 1.0
CE1 B:HIS178 4.4 43.9 1.0
CG B:ASP45 4.4 25.9 1.0
N B:TYR121 4.4 40.7 1.0
OE1 B:GLU34 4.5 37.2 1.0
O B:SER78 4.7 62.4 1.0
CG B:HIS178 4.7 45.4 1.0
CA B:HIS120 4.7 36.8 1.0
ND1 B:HIS120 4.8 34.1 1.0
CB B:TYR121 4.9 49.9 1.0
NE2 B:HIS36 4.9 29.9 1.0
CB B:HIS178 5.0 47.1 1.0
CA B:HIS178 5.0 49.4 1.0

Chlorine binding site 3 out of 6 in 3a6k

Go back to Chlorine Binding Sites List in 3a6k
Chlorine binding site 3 out of 6 in the The E122Q Mutant Creatininase, Mn-Zn Type


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of The E122Q Mutant Creatininase, Mn-Zn Type within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl302

b:48.9
occ:1.00
 MN C:MN300 2.8 38.1 1.0
ZN C:ZN301 2.9 30.2 1.0
ND1 C:HIS178 3.6 45.0 1.0
OE2 C:GLU183 3.8 36.4 1.0
OD1 C:ASP45 3.9 29.8 1.0
OE1 C:GLU183 4.1 36.5 1.0
OD2 C:ASP45 4.1 26.6 1.0
CD C:GLU183 4.2 37.2 1.0
OE1 C:GLU34 4.3 33.9 1.0
CG C:ASP45 4.4 28.6 1.0
CE1 C:HIS178 4.4 44.4 1.0
O C:GLY119 4.4 35.4 1.0
N C:TYR121 4.6 41.5 1.0
CG C:HIS178 4.6 44.9 1.0
NE2 C:HIS36 4.6 30.4 1.0
ND1 C:HIS120 4.7 38.7 1.0
CA C:HIS178 4.8 46.0 1.0
CB C:HIS178 4.8 45.5 1.0
CA C:HIS120 4.8 37.4 1.0
CB C:TYR121 4.8 50.2 1.0
O C:HOH1044 4.9 29.6 1.0
O C:SER78 4.9 62.1 1.0

Chlorine binding site 4 out of 6 in 3a6k

Go back to Chlorine Binding Sites List in 3a6k
Chlorine binding site 4 out of 6 in the The E122Q Mutant Creatininase, Mn-Zn Type


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of The E122Q Mutant Creatininase, Mn-Zn Type within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl302

b:55.6
occ:1.00
 MN D:MN300 3.0 44.7 1.0
ZN D:ZN301 3.3 35.9 1.0
ND1 D:HIS178 3.8 56.5 1.0
OE2 D:GLU183 4.2 42.1 1.0
N D:TYR121 4.2 41.2 1.0
OD1 D:ASP45 4.2 34.1 1.0
OD2 D:ASP45 4.2 33.6 1.0
O D:GLY119 4.2 33.6 1.0
OE1 D:GLU183 4.3 44.5 1.0
CD D:GLU183 4.4 44.9 1.0
O D:SER78 4.6 64.9 1.0
CB D:TYR121 4.6 48.9 1.0
CG D:ASP45 4.6 30.5 1.0
CE1 D:HIS178 4.6 55.9 1.0
CA D:HIS120 4.6 36.8 1.0
OE2 D:GLU34 4.7 36.5 1.0
ND1 D:HIS120 4.8 39.5 1.0
CH2 D:TRP154 4.9 56.9 1.0
CG D:HIS178 4.9 56.2 1.0
CZ3 D:TRP154 4.9 56.6 1.0
C D:HIS120 4.9 38.5 1.0

Chlorine binding site 5 out of 6 in 3a6k

Go back to Chlorine Binding Sites List in 3a6k
Chlorine binding site 5 out of 6 in the The E122Q Mutant Creatininase, Mn-Zn Type


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of The E122Q Mutant Creatininase, Mn-Zn Type within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cl302

b:51.9
occ:1.00
 ZN E:ZN301 2.9 34.6 1.0
MN E:MN300 2.9 38.0 1.0
OD2 E:ASP45 3.8 29.4 1.0
OE2 E:GLU183 3.8 40.7 1.0
ND1 E:HIS178 3.9 47.8 1.0
OD1 E:ASP45 4.0 28.2 1.0
OE1 E:GLU183 4.1 39.5 1.0
CD E:GLU183 4.2 39.8 1.0
CG E:ASP45 4.2 31.6 1.0
O E:GLY119 4.3 35.2 1.0
N E:TYR121 4.5 41.7 1.0
OE1 E:GLU34 4.5 33.2 1.0
O E:SER78 4.7 66.8 1.0
CE1 E:HIS178 4.7 46.2 1.0
O E:HOH1110 4.7 35.9 1.0
NE2 E:HIS36 4.7 27.5 1.0
ND1 E:HIS120 4.7 40.5 1.0
CA E:HIS120 4.8 37.4 1.0
CB E:TYR121 4.8 49.8 1.0
CG E:HIS178 4.9 48.2 1.0

Chlorine binding site 6 out of 6 in 3a6k

Go back to Chlorine Binding Sites List in 3a6k
Chlorine binding site 6 out of 6 in the The E122Q Mutant Creatininase, Mn-Zn Type


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of The E122Q Mutant Creatininase, Mn-Zn Type within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cl302

b:46.2
occ:1.00
 MN F:MN300 2.9 39.0 1.0
ZN F:ZN301 3.0 32.4 1.0
OE2 F:GLU183 3.7 38.4 1.0
OD2 F:ASP45 3.9 26.1 1.0
ND1 F:HIS178 3.9 36.3 1.0
OE1 F:GLU183 3.9 37.4 1.0
OD1 F:ASP45 4.1 30.5 1.0
CD F:GLU183 4.1 40.2 1.0
N F:TYR121 4.3 39.0 1.0
CG F:ASP45 4.3 27.2 1.0
O F:GLY119 4.4 35.3 1.0
O F:SER78 4.5 59.7 1.0
CE1 F:HIS178 4.6 36.2 1.0
OE1 F:GLU34 4.6 35.9 1.0
CB F:TYR121 4.7 45.2 1.0
CA F:HIS120 4.7 36.9 1.0
ND1 F:HIS120 4.8 36.5 1.0
NE2 F:HIS36 4.9 28.5 1.0
O F:HOH1068 4.9 32.4 1.0
CG F:HIS178 5.0 37.6 1.0

Reference:

K.Yamashita, Y.Nakajima, H.Matsushita, Y.Nishiya, R.Yamazawa, Y.F.Wu, F.Matsubara, H.Oyama, K.Ito, T.Yoshimoto. Substitution of GLU122 By Glutamine Revealed the Function of the Second Water Molecule As A Proton Donor in the Binuclear Metal Enzyme Creatininase J.Mol.Biol. V. 396 1081 2010.
ISSN: ISSN 0022-2836
PubMed: 20043918
DOI: 10.1016/J.JMB.2009.12.045
Page generated: Sat Dec 12 09:31:03 2020

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