Atomistry » Zinc » PDB 1p1q-1pe7 » 1p1v
Atomistry »
  Zinc »
    PDB 1p1q-1pe7 »
      1p1v »

Zinc in PDB 1p1v: Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A

Enzymatic activity of Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A

All present enzymatic activity of Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A, PDB code: 1p1v was solved by J.S.Elam, K.Malek, J.A.Rodriguez, P.A.Doucette, A.B.Taylor, L.J.Hayward, D.E.Cabelli, J.S.Valentine, P.J.Hart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.40
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 70.449, 101.140, 143.080, 90.00, 90.00, 90.00
R / Rfree (%) 14.6 / 21.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A (pdb code 1p1v). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A, PDB code: 1p1v:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 1p1v

Go back to Zinc Binding Sites List in 1p1v
Zinc binding site 1 out of 6 in the Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:11.0
occ:1.00
 O1 A:SO4801 2.0 13.2 1.0
ND1 A:HIS46 2.0 10.8 1.0
NE2 A:HIS48 2.0 10.4 1.0
NE2 A:HIS120 2.0 11.9 1.0
CE1 A:HIS48 2.9 11.0 1.0
CE1 A:HIS46 2.9 11.4 1.0
CE1 A:HIS120 2.9 11.7 1.0
CD2 A:HIS120 3.0 11.1 1.0
CG A:HIS46 3.1 11.6 1.0
CD2 A:HIS48 3.2 10.9 1.0
S A:SO4801 3.2 13.4 1.0
CB A:HIS46 3.5 11.0 1.0
O2 A:SO4801 3.5 12.6 1.0
NE2 A:HIS63 3.6 12.1 1.0
CD2 A:HIS63 3.9 13.7 1.0
ND1 A:HIS120 4.0 11.6 1.0
NE2 A:HIS46 4.1 11.7 1.0
O4 A:SO4801 4.1 17.6 1.0
ND1 A:HIS48 4.1 10.6 1.0
O3 A:SO4801 4.1 19.0 1.0
CG A:HIS120 4.1 11.9 1.0
CD2 A:HIS46 4.2 12.5 1.0
CG A:HIS48 4.3 10.4 1.0
O A:HOH823 4.4 19.6 1.0
CG1 A:VAL118 4.5 12.1 1.0
CE1 A:HIS63 4.6 12.6 1.0
NE A:ARG143 4.7 10.6 1.0
CB A:VAL118 4.7 9.4 1.0
CA A:HIS46 4.9 10.1 1.0

Zinc binding site 2 out of 6 in 1p1v

Go back to Zinc Binding Sites List in 1p1v
Zinc binding site 2 out of 6 in the Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn202

b:11.6
occ:1.00
 OD1 A:ASP83 2.0 12.0 1.0
ND1 A:HIS63 2.0 11.1 1.0
ND1 A:HIS80 2.0 13.3 1.0
ND1 A:HIS71 2.0 12.0 1.0
CG A:ASP83 2.7 10.9 1.0
OD2 A:ASP83 2.7 12.0 1.0
CE1 A:HIS71 2.9 11.9 1.0
CE1 A:HIS80 2.9 14.3 1.0
CE1 A:HIS63 2.9 12.6 1.0
CG A:HIS80 3.0 12.9 1.0
CG A:HIS63 3.1 12.4 1.0
CG A:HIS71 3.2 12.0 1.0
CB A:HIS63 3.5 11.8 1.0
CB A:HIS80 3.5 12.0 1.0
CB A:HIS71 3.6 12.7 1.0
CA A:HIS71 3.8 14.3 1.0
NE2 A:HIS80 4.0 14.8 1.0
NE2 A:HIS63 4.1 12.1 1.0
CD2 A:HIS80 4.1 13.2 1.0
NE2 A:HIS71 4.1 12.9 1.0
O A:LYS136 4.1 29.6 1.0
CB A:ASP83 4.1 11.5 1.0
CD2 A:HIS63 4.2 13.7 1.0
CD2 A:HIS71 4.2 13.7 1.0
O A:HOH904 4.4 32.2 1.0
N A:GLY72 4.7 13.2 1.0
N A:HIS80 4.7 11.3 1.0
CA A:ASP83 4.7 10.2 1.0
CA A:HIS80 4.7 11.0 1.0
C A:HIS71 4.8 13.1 1.0
N A:HIS71 4.8 13.5 1.0
N A:ASP83 4.9 10.1 1.0

Zinc binding site 3 out of 6 in 1p1v

Go back to Zinc Binding Sites List in 1p1v
Zinc binding site 3 out of 6 in the Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn203

b:25.1
occ:1.00
 O2 B:SO4802 1.9 30.0 1.0
NE2 B:HIS120 1.9 21.0 1.0
NE2 B:HIS48 2.0 23.4 1.0
ND1 B:HIS46 2.0 22.4 1.0
CE1 B:HIS120 2.7 19.7 1.0
CE1 B:HIS48 2.8 27.1 1.0
CE1 B:HIS46 2.9 25.6 1.0
CD2 B:HIS120 3.0 20.3 1.0
S B:SO4802 3.1 32.2 1.0
CG B:HIS46 3.1 23.1 1.0
CD2 B:HIS48 3.2 22.9 1.0
O3 B:SO4802 3.3 30.6 1.0
NE2 B:HIS63 3.4 29.3 1.0
CB B:HIS46 3.5 22.6 1.0
CD2 B:HIS63 3.8 29.8 1.0
ND1 B:HIS120 3.9 20.9 1.0
ND1 B:HIS48 4.0 27.5 1.0
O4 B:SO4802 4.0 43.6 1.0
CG B:HIS120 4.1 20.2 1.0
O1 B:SO4802 4.1 50.5 1.0
NE2 B:HIS46 4.1 24.0 1.0
CD2 B:HIS46 4.2 23.0 1.0
CG B:HIS48 4.2 23.3 1.0
CE1 B:HIS63 4.5 31.8 1.0
O B:HOH881 4.6 33.6 1.0
CG1 B:VAL118 4.6 19.2 1.0
CB B:VAL118 4.7 18.0 1.0
NE B:ARG143 4.7 25.8 1.0
CA B:HIS46 4.9 21.6 1.0
CG B:ARG143 4.9 25.7 1.0
CG B:HIS63 5.0 29.9 1.0

Zinc binding site 4 out of 6 in 1p1v

Go back to Zinc Binding Sites List in 1p1v
Zinc binding site 4 out of 6 in the Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn204

b:34.0
occ:1.00
 OD1 B:ASP83 1.8 31.8 1.0
ND1 B:HIS80 2.0 37.3 1.0
ND1 B:HIS63 2.0 34.4 1.0
ND1 B:HIS71 2.1 34.3 1.0
CG B:ASP83 2.6 30.1 1.0
OD2 B:ASP83 2.6 33.5 1.0
CE1 B:HIS80 2.9 37.6 1.0
CE1 B:HIS71 2.9 33.1 1.0
CE1 B:HIS63 2.9 31.8 1.0
CG B:HIS80 3.0 36.2 1.0
CG B:HIS63 3.1 29.9 1.0
CG B:HIS71 3.2 37.4 1.0
CB B:HIS80 3.4 37.2 1.0
CB B:HIS63 3.5 29.0 1.0
CB B:HIS71 3.7 39.9 1.0
CA B:HIS71 3.9 42.0 1.0
NE2 B:HIS80 4.0 39.0 1.0
CB B:ASP83 4.0 28.1 1.0
CD2 B:HIS80 4.1 36.6 1.0
NE2 B:HIS71 4.1 33.0 1.0
NE2 B:HIS63 4.1 29.3 1.0
CD2 B:HIS63 4.2 29.8 1.0
CD2 B:HIS71 4.3 37.4 1.0
N B:HIS80 4.5 37.5 1.0
N B:GLY72 4.5 43.3 1.0
CA B:HIS80 4.6 37.4 1.0
CA B:ASP83 4.7 27.0 1.0
C B:HIS71 4.8 41.3 1.0
CB B:THR137 4.8 72.5 1.0
N B:HIS71 4.9 40.9 1.0
N B:ASP83 4.9 32.0 1.0
O B:GLY72 4.9 40.0 1.0

Zinc binding site 5 out of 6 in 1p1v

Go back to Zinc Binding Sites List in 1p1v
Zinc binding site 5 out of 6 in the Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn205

b:9.8
occ:1.00
 O1 C:SO4803 2.0 10.2 1.0
ND1 C:HIS46 2.0 9.1 1.0
NE2 C:HIS48 2.0 9.2 1.0
NE2 C:HIS120 2.0 10.1 1.0
CE1 C:HIS48 2.9 9.2 1.0
CE1 C:HIS120 2.9 10.0 1.0
CE1 C:HIS46 2.9 10.1 1.0
CD2 C:HIS120 3.1 9.6 1.0
CG C:HIS46 3.1 10.0 1.0
CD2 C:HIS48 3.2 9.4 1.0
S C:SO4803 3.2 11.7 1.0
CB C:HIS46 3.5 10.5 1.0
O3 C:SO4803 3.5 11.6 1.0
NE2 C:HIS63 3.5 10.5 1.0
CD2 C:HIS63 3.9 9.6 1.0
ND1 C:HIS120 4.1 10.4 1.0
ND1 C:HIS48 4.1 8.8 1.0
O2 C:SO4803 4.1 17.7 1.0
NE2 C:HIS46 4.1 10.3 1.0
CG C:HIS120 4.2 10.1 1.0
O4 C:SO4803 4.2 18.2 1.0
CD2 C:HIS46 4.2 9.2 1.0
CG C:HIS48 4.2 8.8 1.0
O C:HOH819 4.4 18.5 1.0
CG1 C:VAL118 4.5 11.1 1.0
CE1 C:HIS63 4.6 11.1 1.0
CB C:VAL118 4.6 9.4 1.0
NE C:ARG143 4.7 10.1 1.0
CA C:HIS46 4.9 8.9 1.0

Zinc binding site 6 out of 6 in 1p1v

Go back to Zinc Binding Sites List in 1p1v
Zinc binding site 6 out of 6 in the Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125H to 1.4A within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn206

b:10.3
occ:1.00
 OD1 C:ASP83 2.0 11.4 1.0
ND1 C:HIS80 2.0 10.7 1.0
ND1 C:HIS71 2.0 11.0 1.0
ND1 C:HIS63 2.0 10.2 1.0
CG C:ASP83 2.7 10.8 1.0
OD2 C:ASP83 2.8 11.5 1.0
CE1 C:HIS71 2.9 10.7 1.0
CE1 C:HIS80 2.9 11.0 1.0
CE1 C:HIS63 2.9 11.1 1.0
CG C:HIS80 3.0 11.3 1.0
CG C:HIS63 3.1 9.6 1.0
CG C:HIS71 3.2 11.1 1.0
CB C:HIS80 3.5 11.0 1.0
CB C:HIS63 3.5 11.2 1.0
CB C:HIS71 3.6 11.3 1.0
CA C:HIS71 3.9 12.5 1.0
O C:LYS136 4.0 30.5 1.0
NE2 C:HIS80 4.0 11.7 1.0
NE2 C:HIS71 4.1 11.9 1.0
CD2 C:HIS80 4.1 11.7 1.0
NE2 C:HIS63 4.1 10.5 1.0
CB C:ASP83 4.2 10.9 1.0
CD2 C:HIS63 4.2 9.6 1.0
CD2 C:HIS71 4.2 13.3 1.0
O C:HOH864 4.5 24.5 1.0
N C:GLY72 4.7 11.4 1.0
N C:HIS80 4.7 10.9 1.0
CA C:ASP83 4.7 9.7 1.0
CA C:HIS80 4.8 12.1 1.0
C C:HIS71 4.8 12.7 1.0
N C:HIS71 4.9 13.2 1.0
N C:ASP83 4.9 10.1 1.0
O C:GLY72 5.0 13.1 1.0

Reference:

J.S.Elam, K.Malek, J.A.Rodriguez, P.A.Doucette, A.B.Taylor, L.J.Hayward, D.E.Cabelli, J.S.Valentine, P.J.Hart. An Alternative Mechanism of Bicarbonate-Mediated Peroxidation By Copper-Zinc Superoxide Dismutase: Rates Enhanced Via Proposed Enzyme-Associated Peroxycarbonate Intermediate J.Biol.Chem. V. 278 21032 2003.
ISSN: ISSN 0021-9258
PubMed: 12649272
DOI: 10.1074/JBC.M300484200
Page generated: Wed Dec 16 03:00:26 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy