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Chlorine in PDB 3a6h: W154A Mutant Creatininase

Enzymatic activity of W154A Mutant Creatininase

All present enzymatic activity of W154A Mutant Creatininase:
3.5.2.10;

Protein crystallography data

The structure of W154A Mutant Creatininase, PDB code: 3a6h 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 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 106.800, 60.240, 146.200, 90.00, 100.30, 90.00
R / Rfree (%) 19.9 / 23.1

Other elements in 3a6h:

The structure of W154A Mutant Creatininase 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 W154A Mutant Creatininase (pdb code 3a6h). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the W154A Mutant Creatininase, PDB code: 3a6h:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in 3a6h

Go back to Chlorine Binding Sites List in 3a6h
Chlorine binding site 1 out of 6 in the W154A Mutant Creatininase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of W154A Mutant Creatininase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:33.3
occ:1.00
 MN A:MN300 3.2 36.3 1.0
ZN A:ZN301 3.3 33.1 1.0
O A:HOH1001 3.6 19.7 1.0
N A:TYR121 3.9 26.3 1.0
O A:GLY119 3.9 23.6 1.0
OD1 A:ASP45 4.2 17.0 1.0
OE1 A:GLU183 4.2 25.2 1.0
CA A:HIS120 4.3 27.8 1.0
OD2 A:ASP45 4.4 18.5 1.0
CB A:TYR121 4.5 30.0 1.0
ND1 A:HIS178 4.6 19.7 1.0
CG A:ASP45 4.6 17.4 1.0
CD A:GLU183 4.7 23.0 1.0
C A:HIS120 4.7 27.5 1.0
O A:HOH1617 4.7 39.1 1.0
C A:GLY119 4.7 24.7 1.0
OE2 A:GLU183 4.8 23.3 1.0
CA A:TYR121 4.8 27.1 1.0
ND1 A:HIS120 4.9 26.7 1.0
N A:HIS120 4.9 25.4 1.0
O A:HOH1234 4.9 25.7 1.0

Chlorine binding site 2 out of 6 in 3a6h

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Chlorine binding site 2 out of 6 in the W154A Mutant Creatininase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of W154A Mutant Creatininase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl303

b:32.0
occ:1.00
 MN B:MN300 3.2 39.0 1.0
ZN B:ZN301 3.3 33.8 1.0
O B:GLY119 3.8 27.4 1.0
O B:HOH1002 3.8 17.8 1.0
N B:TYR121 3.9 25.1 1.0
OD1 B:ASP45 4.2 18.6 1.0
OD2 B:ASP45 4.2 18.0 1.0
CA B:HIS120 4.2 25.9 1.0
OE1 B:GLU183 4.3 23.3 1.0
CB B:TYR121 4.5 29.6 1.0
CG B:ASP45 4.5 18.7 1.0
C B:HIS120 4.6 25.7 1.0
C B:GLY119 4.6 25.5 1.0
ND1 B:HIS178 4.7 22.5 1.0
CD B:GLU183 4.8 23.8 1.0
O B:HOH1184 4.8 31.6 1.0
CA B:TYR121 4.8 26.4 1.0
N B:HIS120 4.8 26.4 1.0
OE2 B:GLU183 4.9 22.9 1.0
ND1 B:HIS120 4.9 23.2 1.0

Chlorine binding site 3 out of 6 in 3a6h

Go back to Chlorine Binding Sites List in 3a6h
Chlorine binding site 3 out of 6 in the W154A Mutant Creatininase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of W154A Mutant Creatininase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl304

b:29.4
occ:1.00
 MN C:MN300 3.1 44.6 1.0
ZN C:ZN301 3.3 37.7 1.0
O C:GLY119 3.7 32.3 1.0
O C:HOH1003 3.7 20.3 1.0
N C:TYR121 3.9 27.7 1.0
CA C:HIS120 4.2 28.7 1.0
OE1 C:GLU183 4.2 29.9 1.0
OD2 C:ASP45 4.2 23.2 1.0
OD1 C:ASP45 4.3 23.2 1.0
CB C:TYR121 4.5 32.5 1.0
C C:GLY119 4.5 30.3 1.0
C C:HIS120 4.6 28.7 1.0
CG C:ASP45 4.6 23.4 1.0
N C:HIS120 4.8 30.4 1.0
ND1 C:HIS120 4.8 25.9 1.0
O C:HOH1314 4.8 38.8 1.0
ND1 C:HIS178 4.8 27.3 1.0
CA C:TYR121 4.8 29.0 1.0
CD C:GLU183 4.8 27.2 1.0
OE2 C:GLU183 5.0 29.2 1.0

Chlorine binding site 4 out of 6 in 3a6h

Go back to Chlorine Binding Sites List in 3a6h
Chlorine binding site 4 out of 6 in the W154A Mutant Creatininase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of W154A Mutant Creatininase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl305

b:35.1
occ:1.00
 MN D:MN300 3.2 38.7 1.0
ZN D:ZN301 3.2 35.2 1.0
O D:HOH1004 3.5 17.8 1.0
O D:GLY119 3.8 26.2 1.0
N D:TYR121 4.0 26.4 1.0
OD1 D:ASP45 4.2 20.1 1.0
CA D:HIS120 4.3 27.2 1.0
OE1 D:GLU183 4.3 25.6 1.0
OD2 D:ASP45 4.3 20.4 1.0
ND1 D:HIS178 4.5 22.0 1.0
CB D:TYR121 4.5 31.5 1.0
CG D:ASP45 4.6 19.5 1.0
C D:GLY119 4.7 26.1 1.0
C D:HIS120 4.7 26.8 1.0
CD D:GLU183 4.7 23.9 1.0
OE2 D:GLU183 4.7 26.3 1.0
O D:HOH1262 4.8 30.6 1.0
ND1 D:HIS120 4.9 25.1 1.0
N D:HIS120 4.9 25.2 1.0
CA D:TYR121 4.9 27.6 1.0

Chlorine binding site 5 out of 6 in 3a6h

Go back to Chlorine Binding Sites List in 3a6h
Chlorine binding site 5 out of 6 in the W154A Mutant Creatininase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of W154A Mutant Creatininase within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cl306

b:37.7
occ:1.00
 MN E:MN300 3.0 54.9 1.0
ZN E:ZN301 3.2 45.4 1.0
O E:HOH1005 3.8 30.4 1.0
O E:GLY119 3.9 30.5 1.0
OE1 E:GLU183 3.9 36.2 1.0
OD1 E:ASP45 3.9 30.3 1.0
N E:TYR121 4.1 33.4 1.0
OD2 E:ASP45 4.3 28.6 1.0
CA E:HIS120 4.4 31.5 1.0
CG E:ASP45 4.4 27.9 1.0
ND1 E:HIS178 4.5 36.7 1.0
CB E:TYR121 4.6 37.7 1.0
C E:GLY119 4.7 30.7 1.0
C E:HIS120 4.8 32.3 1.0
CD E:GLU183 4.8 37.4 1.0
ND1 E:HIS120 5.0 30.1 1.0
N E:HIS120 5.0 30.4 1.0
CA E:TYR121 5.0 34.6 1.0

Chlorine binding site 6 out of 6 in 3a6h

Go back to Chlorine Binding Sites List in 3a6h
Chlorine binding site 6 out of 6 in the W154A Mutant Creatininase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of W154A Mutant Creatininase within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cl307

b:47.7
occ:1.00
 MN F:MN300 2.9 52.1 1.0
ZN F:ZN301 3.2 45.7 1.0
O F:HOH1006 3.5 24.1 1.0
O F:GLY119 3.9 32.4 1.0
N F:TYR121 4.0 33.7 1.0
OE1 F:GLU183 4.1 32.8 1.0
OD2 F:ASP45 4.1 29.1 1.0
OD1 F:ASP45 4.2 29.5 1.0
CA F:HIS120 4.4 33.5 1.0
CB F:TYR121 4.5 37.1 1.0
CG F:ASP45 4.5 28.7 1.0
ND1 F:HIS178 4.5 35.1 1.0
C F:HIS120 4.7 33.6 1.0
C F:GLY119 4.8 32.3 1.0
CD F:GLU183 4.8 33.5 1.0
OE2 F:GLU183 4.9 33.5 1.0
CA F:TYR121 4.9 34.0 1.0
ND1 F:HIS120 4.9 31.6 1.0
N F:HIS120 5.0 31.7 1.0
OE2 F:GLU34 5.0 28.7 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: Fri Jul 11 03:00:04 2025

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