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Manganese in PDB 3a6e: W174F Mutant Creatininase, Type I

Enzymatic activity of W174F Mutant Creatininase, Type I

All present enzymatic activity of W174F Mutant Creatininase, Type I:
3.5.2.10;

Protein crystallography data

The structure of W174F Mutant Creatininase, Type I, PDB code: 3a6e 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 (°) 105.900, 59.700, 145.100, 90.00, 99.70, 90.00
R / Rfree (%) 19.6 / 22.9

Other elements in 3a6e:

The structure of W174F Mutant Creatininase, Type I also contains other interesting chemical elements:

Arsenic (As) 6 atoms
Zinc (Zn) 6 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the W174F Mutant Creatininase, Type I (pdb code 3a6e). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the W174F Mutant Creatininase, Type I, PDB code: 3a6e:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6;

Manganese binding site 1 out of 6 in 3a6e

Go back to Manganese Binding Sites List in 3a6e
Manganese binding site 1 out of 6 in the W174F Mutant Creatininase, Type I


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of W174F Mutant Creatininase, Type I within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn300

b:29.1
occ:1.00
 OD2 A:ASP45 2.1 11.9 1.0
O A:HOH1082 2.1 13.2 1.0
OE1 A:GLU34 2.2 14.5 1.0
ND1 A:HIS120 2.2 13.8 1.0
O1 A:CAC302 2.3 23.9 1.0
O2 A:CAC302 2.7 21.6 1.0
CE1 A:HIS120 3.0 14.2 1.0
AS A:CAC302 3.0 27.5 1.0
CD A:GLU34 3.2 14.9 1.0
CG A:ASP45 3.2 13.0 1.0
CG A:HIS120 3.4 14.4 1.0
OE2 A:GLU34 3.4 14.3 1.0
OD1 A:ASP45 3.7 11.8 1.0
ZN A:ZN301 3.7 18.0 1.0
CA A:HIS120 3.8 14.3 1.0
CB A:HIS120 3.9 13.2 1.0
OE1 A:GLU122 4.0 14.9 1.0
NE2 A:HIS120 4.2 14.5 1.0
C1 A:CAC302 4.3 22.8 1.0
N A:TYR121 4.3 14.6 1.0
ND1 A:HIS178 4.3 14.0 1.0
CE1 A:HIS178 4.4 13.7 1.0
CD2 A:HIS120 4.4 11.8 1.0
C A:HIS120 4.5 12.9 1.0
CB A:ASP45 4.5 10.5 1.0
CG A:GLU34 4.5 13.2 1.0
CE1 A:HIS36 4.6 13.4 1.0
C2 A:CAC302 4.6 22.3 1.0
O A:GLY119 4.6 12.7 1.0
NE2 A:HIS36 4.7 10.9 1.0
CB A:GLU34 4.8 13.2 1.0
CD A:GLU122 4.8 16.2 1.0
N A:HIS120 5.0 13.0 1.0
OE2 A:GLU122 5.0 15.8 1.0

Manganese binding site 2 out of 6 in 3a6e

Go back to Manganese Binding Sites List in 3a6e
Manganese binding site 2 out of 6 in the W174F Mutant Creatininase, Type I


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of W174F Mutant Creatininase, Type I within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn300

b:30.7
occ:1.00
 OD2 B:ASP45 2.1 13.7 1.0
OE2 B:GLU34 2.2 15.5 1.0
O B:HOH1135 2.2 15.1 1.0
ND1 B:HIS120 2.3 12.6 1.0
O1 B:CAC303 2.3 25.7 1.0
O2 B:CAC303 2.6 23.9 1.0
CE1 B:HIS120 3.0 11.3 1.0
AS B:CAC303 3.1 27.6 1.0
CD B:GLU34 3.1 15.2 1.0
CG B:ASP45 3.2 14.5 1.0
OE1 B:GLU34 3.4 15.8 1.0
CG B:HIS120 3.5 13.2 1.0
ZN B:ZN301 3.7 19.9 1.0
OD1 B:ASP45 3.7 14.4 1.0
CA B:HIS120 3.9 15.4 1.0
CB B:HIS120 4.0 14.4 1.0
OE1 B:GLU122 4.0 17.6 1.0
NE2 B:HIS120 4.2 13.1 1.0
ND1 B:HIS178 4.3 14.6 1.0
C1 B:CAC303 4.3 25.2 1.0
CE1 B:HIS178 4.3 16.9 1.0
N B:TYR121 4.4 14.8 1.0
CB B:ASP45 4.4 15.0 1.0
CD2 B:HIS120 4.5 10.7 1.0
CG B:GLU34 4.5 12.7 1.0
NE2 B:HIS36 4.6 11.5 1.0
C2 B:CAC303 4.6 26.4 1.0
O B:GLY119 4.6 12.3 1.0
C B:HIS120 4.6 15.8 1.0
CE1 B:HIS36 4.6 13.9 1.0
CB B:GLU34 4.7 11.5 1.0
CD B:GLU122 4.9 16.4 1.0

Manganese binding site 3 out of 6 in 3a6e

Go back to Manganese Binding Sites List in 3a6e
Manganese binding site 3 out of 6 in the W174F Mutant Creatininase, Type I


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of W174F Mutant Creatininase, Type I within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn300

b:36.6
occ:1.00
 OD2 C:ASP45 2.1 16.9 1.0
OE2 C:GLU34 2.2 17.4 1.0
ND1 C:HIS120 2.2 15.5 1.0
O C:HOH1177 2.3 17.1 1.0
O2 C:CAC304 2.4 31.6 1.0
O1 C:CAC304 2.6 26.1 1.0
CE1 C:HIS120 2.9 13.6 1.0
CD C:GLU34 3.1 16.6 1.0
AS C:CAC304 3.1 31.8 1.0
CG C:ASP45 3.2 19.5 1.0
OE1 C:GLU34 3.4 17.5 1.0
CG C:HIS120 3.4 15.3 1.0
OD1 C:ASP45 3.7 18.3 1.0
ZN C:ZN301 3.8 23.4 1.0
CA C:HIS120 3.9 17.5 1.0
CB C:HIS120 3.9 16.9 1.0
OE1 C:GLU122 4.1 18.0 1.0
NE2 C:HIS120 4.2 15.8 1.0
C2 C:CAC304 4.3 29.8 1.0
ND1 C:HIS178 4.3 21.2 1.0
CE1 C:HIS178 4.3 22.6 1.0
CD2 C:HIS120 4.4 12.8 1.0
CG C:GLU34 4.4 15.1 1.0
CB C:ASP45 4.4 17.4 1.0
N C:TYR121 4.4 16.4 1.0
CE1 C:HIS36 4.6 16.8 1.0
C C:HIS120 4.6 18.1 1.0
O C:GLY119 4.6 18.6 1.0
NE2 C:HIS36 4.6 15.0 1.0
CB C:GLU34 4.6 14.2 1.0
C1 C:CAC304 4.6 30.0 1.0
CD C:GLU122 4.9 17.9 1.0

Manganese binding site 4 out of 6 in 3a6e

Go back to Manganese Binding Sites List in 3a6e
Manganese binding site 4 out of 6 in the W174F Mutant Creatininase, Type I


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of W174F Mutant Creatininase, Type I within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn300

b:32.8
occ:1.00
 OD2 D:ASP45 2.1 14.8 1.0
O D:HOH1074 2.2 13.1 1.0
OE2 D:GLU34 2.2 19.4 1.0
O2 D:CAC305 2.3 29.6 1.0
ND1 D:HIS120 2.3 15.9 1.0
O1 D:CAC305 2.5 25.0 1.0
AS D:CAC305 3.0 30.8 1.0
CE1 D:HIS120 3.1 19.1 1.0
CD D:GLU34 3.2 16.4 1.0
CG D:ASP45 3.2 15.2 1.0
OE1 D:GLU34 3.5 18.3 1.0
CG D:HIS120 3.5 16.5 1.0
ZN D:ZN301 3.6 22.3 1.0
OD1 D:ASP45 3.7 14.3 1.0
CA D:HIS120 3.8 16.5 1.0
CB D:HIS120 4.0 16.1 1.0
OE1 D:GLU122 4.0 16.6 1.0
C2 D:CAC305 4.2 27.7 1.0
NE2 D:HIS120 4.3 17.2 1.0
ND1 D:HIS178 4.3 14.4 1.0
CE1 D:HIS178 4.3 14.3 1.0
N D:TYR121 4.4 16.3 1.0
CB D:ASP45 4.5 14.4 1.0
C1 D:CAC305 4.5 27.1 1.0
C D:HIS120 4.5 16.0 1.0
O D:GLY119 4.5 17.4 1.0
CD2 D:HIS120 4.5 14.8 1.0
CE1 D:HIS36 4.5 17.2 1.0
NE2 D:HIS36 4.5 13.7 1.0
CG D:GLU34 4.5 17.7 1.0
CB D:GLU34 4.8 16.6 1.0
CD D:GLU122 4.9 18.8 1.0
N D:HIS120 5.0 16.5 1.0

Manganese binding site 5 out of 6 in 3a6e

Go back to Manganese Binding Sites List in 3a6e
Manganese binding site 5 out of 6 in the W174F Mutant Creatininase, Type I


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of W174F Mutant Creatininase, Type I within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn300

b:41.4
occ:1.00
 OD2 E:ASP45 2.2 22.6 1.0
OE2 E:GLU34 2.2 22.0 1.0
O E:HOH1289 2.2 18.7 1.0
ND1 E:HIS120 2.3 24.3 1.0
O1 E:CAC306 2.3 40.4 1.0
O2 E:CAC306 2.7 35.5 1.0
CE1 E:HIS120 3.0 24.9 1.0
AS E:CAC306 3.1 40.5 1.0
CG E:ASP45 3.2 22.1 1.0
CD E:GLU34 3.2 21.7 1.0
CG E:HIS120 3.4 25.0 1.0
OE1 E:GLU34 3.6 23.7 1.0
OD1 E:ASP45 3.6 23.7 1.0
ZN E:ZN301 3.8 27.2 1.0
CA E:HIS120 3.8 23.4 1.0
CB E:HIS120 3.9 24.7 1.0
OE1 E:GLU122 4.0 25.2 1.0
NE2 E:HIS120 4.2 23.8 1.0
ND1 E:HIS178 4.4 29.8 1.0
C1 E:CAC306 4.4 38.4 1.0
N E:TYR121 4.4 24.2 1.0
CE1 E:HIS178 4.4 27.8 1.0
CB E:ASP45 4.4 19.3 1.0
CD2 E:HIS120 4.5 22.5 1.0
O E:GLY119 4.5 19.6 1.0
CG E:GLU34 4.5 22.5 1.0
C E:HIS120 4.6 24.9 1.0
C2 E:CAC306 4.6 39.6 1.0
CB E:GLU34 4.6 21.6 1.0
CE1 E:HIS36 4.6 21.8 1.0
NE2 E:HIS36 4.7 21.8 1.0
CD E:GLU122 4.9 23.1 1.0
N E:HIS120 5.0 22.0 1.0

Manganese binding site 6 out of 6 in 3a6e

Go back to Manganese Binding Sites List in 3a6e
Manganese binding site 6 out of 6 in the W174F Mutant Creatininase, Type I


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of W174F Mutant Creatininase, Type I within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mn300

b:45.8
occ:1.00
 OE2 F:GLU34 2.2 21.9 1.0
OD2 F:ASP45 2.2 21.5 1.0
ND1 F:HIS120 2.3 21.3 1.0
O1 F:CAC307 2.3 39.1 1.0
O F:HOH1246 2.4 23.8 1.0
O2 F:CAC307 2.6 35.3 1.0
CE1 F:HIS120 3.0 22.0 1.0
AS F:CAC307 3.1 39.5 1.0
CG F:ASP45 3.2 22.2 1.0
CD F:GLU34 3.2 20.7 1.0
CG F:HIS120 3.5 23.0 1.0
OE1 F:GLU34 3.6 21.2 1.0
OD1 F:ASP45 3.6 23.0 1.0
ZN F:ZN301 3.8 26.1 1.0
CA F:HIS120 3.9 21.8 1.0
CB F:HIS120 4.0 22.9 1.0
OE1 F:GLU122 4.1 22.1 1.0
NE2 F:HIS120 4.2 22.4 1.0
ND1 F:HIS178 4.4 23.3 1.0
C1 F:CAC307 4.4 37.8 1.0
CE1 F:HIS178 4.4 19.5 1.0
N F:TYR121 4.4 23.7 1.0
CB F:ASP45 4.4 20.0 1.0
CD2 F:HIS120 4.5 20.7 1.0
C2 F:CAC307 4.5 37.3 1.0
CG F:GLU34 4.5 20.4 1.0
O F:GLY119 4.5 21.0 1.0
CE1 F:HIS36 4.6 19.9 1.0
C F:HIS120 4.6 23.2 1.0
NE2 F:HIS36 4.6 19.4 1.0
CB F:GLU34 4.7 18.0 1.0
CD F:GLU122 4.9 21.8 1.0
OE2 F:GLU122 4.9 20.5 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 Oct 5 15:39:59 2024

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