Atomistry » Arsenic » PDB 2xod-3g2f » 3a6e
Atomistry »
  Arsenic »
    PDB 2xod-3g2f »
      3a6e »

Arsenic 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:

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

Arsenic Binding Sites:

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

Arsenic binding site 1 out of 6 in 3a6e

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


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of W174F Mutant Creatininase, Type I within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As302

b:27.5
occ:1.00
 AS A:CAC302 0.0 27.5 1.0
O2 A:CAC302 1.7 21.6 1.0
O1 A:CAC302 1.7 23.9 1.0
C1 A:CAC302 2.0 22.8 1.0
C2 A:CAC302 2.0 22.3 1.0
MN A:MN300 3.0 29.1 1.0
ZN A:ZN301 3.3 18.0 1.0
O A:HOH1082 3.4 13.2 1.0
N A:TYR121 4.0 14.6 1.0
OE1 A:GLU183 4.1 15.7 1.0
OD2 A:ASP45 4.1 11.9 1.0
OD1 A:ASP45 4.1 11.8 1.0
ND1 A:HIS178 4.2 14.0 1.0
O A:GLY119 4.2 12.7 1.0
CB A:TYR121 4.4 17.6 1.0
CD A:GLU183 4.5 18.9 1.0
CG A:ASP45 4.5 13.0 1.0
OE2 A:GLU183 4.5 15.7 1.0
CA A:HIS120 4.5 14.3 1.0
O A:GLU177 4.5 25.3 1.0
OE1 A:GLU34 4.7 14.5 1.0
O A:SER78 4.8 19.1 1.0
C A:HIS120 4.8 12.9 1.0
ND1 A:HIS120 4.8 13.8 1.0
CA A:TYR121 4.9 15.2 1.0
O A:HOH1165 4.9 18.4 1.0
CZ3 A:TRP154 4.9 20.6 1.0
CH2 A:TRP154 4.9 17.2 1.0
OE1 A:GLU122 5.0 14.9 1.0

Arsenic binding site 2 out of 6 in 3a6e

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


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of W174F Mutant Creatininase, Type I within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As303

b:27.6
occ:1.00
 AS B:CAC303 0.0 27.6 1.0
O2 B:CAC303 1.7 23.9 1.0
O1 B:CAC303 1.7 25.7 1.0
C1 B:CAC303 2.0 25.2 1.0
C2 B:CAC303 2.0 26.4 1.0
MN B:MN300 3.1 30.7 1.0
ZN B:ZN301 3.3 19.9 1.0
O B:HOH1135 3.5 15.1 1.0
OD2 B:ASP45 4.0 13.7 1.0
OE1 B:GLU183 4.0 16.6 1.0
N B:TYR121 4.1 14.8 1.0
ND1 B:HIS178 4.1 14.6 1.0
OD1 B:ASP45 4.2 14.4 1.0
O B:GLY119 4.2 12.3 1.0
CG B:ASP45 4.5 14.5 1.0
CD B:GLU183 4.5 17.8 1.0
CB B:TYR121 4.5 19.2 1.0
OE2 B:GLU183 4.5 16.4 1.0
O B:GLU177 4.6 25.1 1.0
CA B:HIS120 4.6 15.4 1.0
OE2 B:GLU34 4.8 15.5 1.0
ND1 B:HIS120 4.8 12.6 1.0
O B:SER78 4.8 18.5 1.0
O B:HOH1189 4.8 18.3 1.0
O B:HOH1749 4.9 30.4 1.0
C B:HIS120 4.9 15.8 1.0
CH2 B:TRP154 4.9 19.1 1.0
CZ3 B:TRP154 4.9 20.0 1.0
CA B:TYR121 5.0 16.4 1.0
CE1 B:HIS178 5.0 16.9 1.0

Arsenic binding site 3 out of 6 in 3a6e

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


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of W174F Mutant Creatininase, Type I within 5.0Å range:
probe atom residue distance (Å) B Occ
C:As304

b:31.8
occ:1.00
 AS C:CAC304 0.0 31.8 1.0
O1 C:CAC304 1.7 26.1 1.0
O2 C:CAC304 1.7 31.6 1.0
C1 C:CAC304 2.0 30.0 1.0
C2 C:CAC304 2.0 29.8 1.0
MN C:MN300 3.1 36.6 1.0
ZN C:ZN301 3.3 23.4 1.0
O C:HOH1177 3.4 17.1 1.0
OE1 C:GLU183 4.1 21.9 1.0
N C:TYR121 4.1 16.4 1.0
ND1 C:HIS178 4.1 21.2 1.0
OD2 C:ASP45 4.1 16.9 1.0
OD1 C:ASP45 4.2 18.3 1.0
O C:GLY119 4.2 18.6 1.0
OE2 C:GLU183 4.5 20.2 1.0
CB C:TYR121 4.5 21.6 1.0
O C:GLU177 4.5 27.7 1.0
CG C:ASP45 4.5 19.5 1.0
CD C:GLU183 4.5 21.6 1.0
CA C:HIS120 4.6 17.5 1.0
OE2 C:GLU34 4.7 17.4 1.0
ND1 C:HIS120 4.8 15.5 1.0
O C:SER78 4.8 21.6 1.0
CH2 C:TRP154 4.8 24.9 1.0
O C:HOH1234 4.9 21.2 1.0
CZ3 C:TRP154 4.9 25.0 1.0
C C:HIS120 4.9 18.1 1.0
CE1 C:HIS178 5.0 22.6 1.0
CA C:TYR121 5.0 18.6 1.0
OE1 C:GLU122 5.0 18.0 1.0

Arsenic binding site 4 out of 6 in 3a6e

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


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 4 of W174F Mutant Creatininase, Type I within 5.0Å range:
probe atom residue distance (Å) B Occ
D:As305

b:30.8
occ:1.00
 AS D:CAC305 0.0 30.8 1.0
O1 D:CAC305 1.7 25.0 1.0
O2 D:CAC305 1.7 29.6 1.0
C1 D:CAC305 2.0 27.1 1.0
C2 D:CAC305 2.0 27.7 1.0
MN D:MN300 3.0 32.8 1.0
ZN D:ZN301 3.3 22.3 1.0
O D:HOH1074 3.4 13.1 1.0
OE1 D:GLU183 4.0 15.9 1.0
OD2 D:ASP45 4.1 14.8 1.0
ND1 D:HIS178 4.1 14.4 1.0
N D:TYR121 4.1 16.3 1.0
OD1 D:ASP45 4.2 14.3 1.0
O D:GLY119 4.2 17.4 1.0
CD D:GLU183 4.4 19.0 1.0
OE2 D:GLU183 4.4 18.0 1.0
CB D:TYR121 4.5 19.7 1.0
CG D:ASP45 4.5 15.2 1.0
O D:GLU177 4.5 26.8 1.0
CA D:HIS120 4.6 16.5 1.0
O D:SER78 4.6 20.1 1.0
OE2 D:GLU34 4.8 19.4 1.0
ND1 D:HIS120 4.8 15.9 1.0
O D:HOH1184 4.9 18.9 1.0
C D:HIS120 4.9 16.0 1.0
CZ3 D:TRP154 4.9 20.9 1.0
CH2 D:TRP154 4.9 19.7 1.0
CE1 D:HIS178 5.0 14.3 1.0
CA D:TYR121 5.0 17.8 1.0
OE1 D:GLU122 5.0 16.6 1.0

Arsenic binding site 5 out of 6 in 3a6e

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


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 5 of W174F Mutant Creatininase, Type I within 5.0Å range:
probe atom residue distance (Å) B Occ
E:As306

b:40.5
occ:1.00
 AS E:CAC306 0.0 40.5 1.0
O2 E:CAC306 1.7 35.5 1.0
O1 E:CAC306 1.7 40.4 1.0
C2 E:CAC306 2.0 39.6 1.0
C1 E:CAC306 2.0 38.4 1.0
MN E:MN300 3.1 41.4 1.0
O E:HOH1289 3.4 18.7 1.0
ZN E:ZN301 3.4 27.2 1.0
OE1 E:GLU183 4.0 31.8 1.0
OD1 E:ASP45 4.1 23.7 1.0
N E:TYR121 4.1 24.2 1.0
O E:GLY119 4.2 19.6 1.0
ND1 E:HIS178 4.2 29.8 1.0
OD2 E:ASP45 4.3 22.6 1.0
CB E:TYR121 4.5 28.5 1.0
CG E:ASP45 4.5 22.1 1.0
CA E:HIS120 4.6 23.4 1.0
O E:GLU177 4.7 39.5 1.0
CD E:GLU183 4.7 31.5 1.0
O E:SER78 4.7 26.9 1.0
CH2 E:TRP154 4.8 35.7 1.0
OE2 E:GLU183 4.8 30.5 1.0
OE2 E:GLU34 4.8 22.0 1.0
CZ3 E:TRP154 4.8 37.3 1.0
ND1 E:HIS120 4.8 24.3 1.0
C E:HIS120 4.9 24.9 1.0
CA E:TYR121 5.0 25.8 1.0
O E:HOH1305 5.0 23.0 1.0

Arsenic binding site 6 out of 6 in 3a6e

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


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 6 of W174F Mutant Creatininase, Type I within 5.0Å range:
probe atom residue distance (Å) B Occ
F:As307

b:39.5
occ:1.00
 AS F:CAC307 0.0 39.5 1.0
O2 F:CAC307 1.7 35.3 1.0
O1 F:CAC307 1.7 39.1 1.0
C2 F:CAC307 2.0 37.3 1.0
C1 F:CAC307 2.0 37.8 1.0
MN F:MN300 3.1 45.8 1.0
ZN F:ZN301 3.4 26.1 1.0
O F:HOH1246 3.5 23.8 1.0
OD1 F:ASP45 4.1 23.0 1.0
N F:TYR121 4.1 23.7 1.0
OE2 F:GLU183 4.2 27.0 1.0
ND1 F:HIS178 4.2 23.3 1.0
O F:GLY119 4.2 21.0 1.0
OD2 F:ASP45 4.4 21.5 1.0
CB F:TYR121 4.4 27.9 1.0
CG F:ASP45 4.6 22.2 1.0
O F:GLU177 4.6 37.5 1.0
OE1 F:GLU183 4.6 25.1 1.0
CA F:HIS120 4.6 21.8 1.0
CD F:GLU183 4.6 26.2 1.0
CH2 F:TRP154 4.7 37.2 1.0
ND1 F:HIS120 4.8 21.3 1.0
OE2 F:GLU34 4.8 21.9 1.0
CZ3 F:TRP154 4.8 37.8 1.0
O F:SER78 4.9 26.4 1.0
C F:HIS120 4.9 23.2 1.0
CA F:TYR121 4.9 24.9 1.0
OE1 F:GLU122 4.9 22.1 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 01:39:31 2020

Last articles

Zn in 7OQY
Zn in 7PEL
Zn in 7OYG
Zn in 7P3S
Zn in 7PE7
Zn in 7RZC
Zn in 7PE9
Zn in 7PE8
Zn in 7RAG
Zn in 7RN5
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy