Atomistry » Zinc » PDB 2ja8-2jt6 » 2jlp
Atomistry »
  Zinc »
    PDB 2ja8-2jt6 »
      2jlp »

Zinc in PDB 2jlp: Crystal Structure of Human Extracellular Copper-Zinc Superoxide Dismutase.

Enzymatic activity of Crystal Structure of Human Extracellular Copper-Zinc Superoxide Dismutase.

All present enzymatic activity of Crystal Structure of Human Extracellular Copper-Zinc Superoxide Dismutase.:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of Human Extracellular Copper-Zinc Superoxide Dismutase., PDB code: 2jlp was solved by S.V.Antonyuk, R.W.Strange, S.L.Marklund, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.20 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 56.738, 93.588, 75.600, 90.00, 106.23, 90.00
R / Rfree (%) 15 / 18.5

Other elements in 2jlp:

The structure of Crystal Structure of Human Extracellular Copper-Zinc Superoxide Dismutase. also contains other interesting chemical elements:

Copper (Cu) 8 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Extracellular Copper-Zinc Superoxide Dismutase. (pdb code 2jlp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Human Extracellular Copper-Zinc Superoxide Dismutase., PDB code: 2jlp:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2jlp

Go back to Zinc Binding Sites List in 2jlp
Zinc binding site 1 out of 4 in the Crystal Structure of Human Extracellular Copper-Zinc Superoxide Dismutase.


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 Human Extracellular Copper-Zinc Superoxide Dismutase. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn226

b:28.7
occ:1.00
 ND1 A:HIS124 2.0 23.3 1.0
ND1 A:HIS113 2.0 27.5 1.0
OD1 A:ASP127 2.1 27.1 1.0
ND1 A:HIS121 2.1 24.4 1.0
CG A:ASP127 2.7 27.4 1.0
OD2 A:ASP127 2.7 27.1 1.0
CE1 A:HIS124 2.8 25.1 1.0
CE1 A:HIS113 2.9 31.3 1.0
CE1 A:HIS121 3.0 26.9 1.0
CG A:HIS113 3.1 27.9 1.0
CG A:HIS124 3.1 24.8 1.0
CG A:HIS121 3.3 26.3 1.0
CB A:HIS113 3.4 26.9 1.0
CB A:HIS124 3.6 27.2 1.0
CB A:HIS121 3.7 26.0 1.0
O A:HOH2105 3.9 23.4 1.0
O A:GLU179 4.0 28.7 1.0
NE2 A:HIS124 4.0 26.6 1.0
NE2 A:HIS113 4.1 34.0 1.0
CB A:ASP127 4.1 28.3 1.0
CD2 A:HIS124 4.2 27.8 1.0
CD2 A:HIS113 4.2 30.7 1.0
NE2 A:HIS121 4.2 25.9 1.0
CA A:HIS121 4.2 27.1 1.0
CD2 A:HIS121 4.3 30.7 1.0
CA A:PRO122 4.7 27.6 1.0
N A:HIS124 4.7 27.5 1.0
CA A:ASP127 4.8 28.5 1.0
CA A:HIS124 4.8 26.4 1.0
CD2 A:HIS96 4.8 31.2 1.0
C A:GLU179 4.9 27.9 1.0
CA A:ASN180 4.9 30.2 1.0
CA A:HIS113 4.9 27.5 1.0
N A:HIS121 5.0 26.7 1.0

Zinc binding site 2 out of 4 in 2jlp

Go back to Zinc Binding Sites List in 2jlp
Zinc binding site 2 out of 4 in the Crystal Structure of Human Extracellular Copper-Zinc Superoxide Dismutase.


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 Human Extracellular Copper-Zinc Superoxide Dismutase. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn226

b:27.4
occ:1.00
 OD1 B:ASP127 2.0 24.4 1.0
ND1 B:HIS113 2.0 26.4 1.0
ND1 B:HIS124 2.0 25.0 1.0
ND1 B:HIS121 2.1 24.6 1.0
CG B:ASP127 2.6 25.6 1.0
OD2 B:ASP127 2.6 26.6 1.0
CE1 B:HIS124 2.9 25.7 1.0
CE1 B:HIS113 2.9 28.2 1.0
CE1 B:HIS121 3.0 24.7 1.0
CG B:HIS113 3.1 22.5 1.0
CG B:HIS124 3.1 27.0 1.0
CG B:HIS121 3.3 26.5 1.0
CB B:HIS113 3.5 26.6 1.0
CB B:HIS124 3.6 28.1 1.0
CB B:HIS121 3.7 25.6 1.0
O B:HOH2098 3.9 22.6 1.0
O B:GLU179 4.0 30.3 1.0
NE2 B:HIS124 4.0 26.1 1.0
NE2 B:HIS113 4.1 28.9 1.0
CB B:ASP127 4.1 27.6 1.0
CA B:HIS121 4.1 26.5 1.0
CD2 B:HIS124 4.2 26.5 1.0
CD2 B:HIS113 4.2 28.7 1.0
NE2 B:HIS121 4.2 26.1 1.0
CD2 B:HIS121 4.3 25.6 1.0
N B:HIS124 4.7 26.4 1.0
CA B:PRO122 4.7 26.2 1.0
CA B:HIS124 4.8 26.7 1.0
CA B:ASP127 4.8 28.8 1.0
CA B:ASN180 4.8 31.3 1.0
C B:GLU179 4.9 31.4 1.0
CD2 B:HIS96 4.9 29.1 1.0
N B:HIS121 5.0 27.1 1.0

Zinc binding site 3 out of 4 in 2jlp

Go back to Zinc Binding Sites List in 2jlp
Zinc binding site 3 out of 4 in the Crystal Structure of Human Extracellular Copper-Zinc Superoxide Dismutase.


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 Human Extracellular Copper-Zinc Superoxide Dismutase. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn226

b:28.0
occ:1.00
 ND1 C:HIS113 2.0 27.1 1.0
ND1 C:HIS124 2.0 25.8 1.0
OD1 C:ASP127 2.1 27.2 1.0
ND1 C:HIS121 2.1 24.4 1.0
OD2 C:ASP127 2.6 27.5 1.0
CG C:ASP127 2.7 28.2 1.0
CE1 C:HIS113 2.9 26.9 1.0
CE1 C:HIS124 2.9 26.1 1.0
CE1 C:HIS121 2.9 24.3 1.0
CG C:HIS113 3.1 25.3 1.0
CG C:HIS124 3.1 25.4 1.0
CG C:HIS121 3.2 25.1 1.0
CB C:HIS113 3.5 26.9 1.0
CB C:HIS124 3.5 26.8 1.0
CB C:HIS121 3.7 25.9 1.0
O C:HOH2104 3.9 24.4 1.0
NE2 C:HIS124 4.1 25.3 1.0
NE2 C:HIS113 4.1 27.3 1.0
O C:GLU179 4.1 31.2 1.0
NE2 C:HIS121 4.1 25.2 1.0
CA C:HIS121 4.1 26.5 1.0
CB C:ASP127 4.2 28.5 1.0
CD2 C:HIS113 4.2 27.3 1.0
CD2 C:HIS124 4.2 27.2 1.0
CD2 C:HIS121 4.3 25.1 1.0
CA C:PRO122 4.7 26.1 1.0
N C:HIS124 4.7 25.9 1.0
CA C:HIS124 4.7 26.5 1.0
CA C:ASN180 4.8 31.3 1.0
CA C:ASP127 4.8 28.9 1.0
C C:GLU179 5.0 31.5 1.0
CD2 C:HIS96 5.0 29.2 1.0

Zinc binding site 4 out of 4 in 2jlp

Go back to Zinc Binding Sites List in 2jlp
Zinc binding site 4 out of 4 in the Crystal Structure of Human Extracellular Copper-Zinc Superoxide Dismutase.


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 Human Extracellular Copper-Zinc Superoxide Dismutase. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn226

b:29.8
occ:1.00
 ND1 D:HIS113 2.0 29.3 1.0
ND1 D:HIS124 2.0 23.4 1.0
OD1 D:ASP127 2.1 28.2 1.0
ND1 D:HIS121 2.1 24.6 1.0
CG D:ASP127 2.7 26.7 1.0
OD2 D:ASP127 2.8 27.8 1.0
CE1 D:HIS124 2.8 28.1 1.0
CE1 D:HIS113 2.9 34.7 1.0
CE1 D:HIS121 3.0 29.0 1.0
CG D:HIS113 3.1 28.6 1.0
CG D:HIS124 3.1 28.4 1.0
CG D:HIS121 3.2 28.1 1.0
CB D:HIS113 3.5 27.4 1.0
CB D:HIS124 3.6 30.1 1.0
CB D:HIS121 3.7 29.4 1.0
O D:HOH2091 3.8 24.3 1.0
O D:GLU179 3.9 33.9 1.0
NE2 D:HIS124 4.0 25.9 1.0
NE2 D:HIS113 4.0 34.2 1.0
CA D:HIS121 4.1 29.8 1.0
CD2 D:HIS124 4.1 30.2 1.0
CD2 D:HIS113 4.1 33.7 1.0
CB D:ASP127 4.1 28.7 1.0
NE2 D:HIS121 4.2 27.5 1.0
CD2 D:HIS121 4.3 28.6 1.0
CA D:ASP127 4.8 28.4 1.0
N D:HIS124 4.8 29.6 1.0
CA D:PRO122 4.8 31.1 1.0
CA D:HIS124 4.8 29.3 1.0
C D:GLU179 4.9 33.0 1.0
CD2 D:HIS96 4.9 30.6 1.0
N D:HIS121 4.9 29.6 1.0
CA D:ASN180 5.0 31.6 1.0
CA D:HIS113 5.0 27.9 1.0

Reference:

S.V.Antonyuk, R.W.Strange, S.L.Marklund, S.S.Hasnain. The Structure of Human Extracellular Copper-Zinc Superoxide Dismutase at 1.7 A Resolution: Insights Into Heparin and Collagen Binding. J.Mol.Biol. V. 388 310 2009.
ISSN: ISSN 0022-2836
PubMed: 19289127
DOI: 10.1016/J.JMB.2009.03.026
Page generated: Thu Oct 17 01:15:44 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy