Atomistry » Copper » PDB 1eso-1haw » 1f1g
Atomistry »
  Copper »
    PDB 1eso-1haw »
      1f1g »

Copper in PDB 1f1g: Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide

Enzymatic activity of Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide

All present enzymatic activity of Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide, PDB code: 1f1g was solved by P.J.Hart, N.L.Ogihara, H.Liu, A.M.Nersissian, J.S.Valentine, D.Eisenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.35
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 72.500, 72.480, 72.470, 109.20, 109.55, 109.21
R / Rfree (%) n/a / n/a

Other elements in 1f1g:

The structure of Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide also contains other interesting chemical elements:

Zinc (Zn) 6 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide (pdb code 1f1g). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide, PDB code: 1f1g:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 1f1g

Go back to Copper Binding Sites List in 1f1g
Copper binding site 1 out of 6 in the Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu4001

b:13.0
occ:1.00
NE2 A:HIS48 1.9 9.7 1.0
ND1 A:HIS46 1.9 11.0 1.0
NE2 A:HIS120 2.0 10.0 1.0
CE1 A:HIS48 2.9 10.1 1.0
CE1 A:HIS46 2.9 10.5 1.0
CD2 A:HIS120 2.9 10.9 1.0
CG A:HIS46 3.0 9.9 1.0
CD2 A:HIS48 3.0 9.3 1.0
CE1 A:HIS120 3.0 10.1 1.0
CB A:HIS46 3.3 11.3 1.0
NE2 A:HIS63 3.4 11.5 1.0
CD2 A:HIS63 3.7 12.6 1.0
O A:HOH3083 3.8 50.0 1.0
O A:HOH3075 3.9 50.0 1.0
CB A:VAL118 3.9 9.8 1.0
ND1 A:HIS48 4.1 9.8 1.0
NE2 A:HIS46 4.1 11.0 1.0
CD2 A:HIS46 4.1 10.5 1.0
N A:HIS46 4.1 8.7 1.0
CG1 A:VAL118 4.1 11.0 1.0
CG A:HIS120 4.1 10.1 1.0
ND1 A:HIS120 4.1 10.6 1.0
CG A:HIS48 4.1 8.2 1.0
CA A:HIS46 4.2 10.3 1.0
CE1 A:HIS63 4.2 10.5 1.0
O A:VAL118 4.4 8.8 1.0
O A:HIS46 4.5 10.1 1.0
C A:HIS46 4.6 8.8 1.0
CG A:HIS63 4.7 9.5 1.0
CG2 A:VAL118 4.7 10.2 1.0
C A:VAL118 4.9 8.1 1.0
ND1 A:HIS63 4.9 11.0 1.0
C A:PHE45 4.9 8.7 1.0
CA A:VAL118 5.0 8.6 1.0

Copper binding site 2 out of 6 in 1f1g

Go back to Copper Binding Sites List in 1f1g
Copper binding site 2 out of 6 in the Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu4003

b:13.1
occ:1.00
NE2 B:HIS203 1.9 10.0 1.0
ND1 B:HIS201 2.0 10.9 1.0
NE2 B:HIS275 2.0 9.4 1.0
CE1 B:HIS203 2.8 9.8 1.0
CE1 B:HIS201 3.0 10.3 1.0
CD2 B:HIS275 3.0 10.2 1.0
CD2 B:HIS203 3.0 9.3 1.0
CG B:HIS201 3.0 9.1 1.0
CE1 B:HIS275 3.1 10.3 1.0
CB B:HIS201 3.3 10.2 1.0
NE2 B:HIS218 3.3 10.8 1.0
CD2 B:HIS218 3.7 10.9 1.0
O B:HOH3077 3.8 50.0 1.0
CB B:VAL273 3.9 9.0 1.0
ND1 B:HIS203 4.0 10.0 1.0
CG1 B:VAL273 4.1 10.9 1.0
CD2 B:HIS201 4.1 11.2 1.0
NE2 B:HIS201 4.1 9.8 1.0
CG B:HIS203 4.1 9.1 1.0
N B:HIS201 4.1 8.1 1.0
CG B:HIS275 4.2 9.2 1.0
ND1 B:HIS275 4.2 10.2 1.0
CE1 B:HIS218 4.2 11.2 1.0
CA B:HIS201 4.2 8.9 1.0
O B:VAL273 4.4 9.6 1.0
O B:HIS201 4.6 10.4 1.0
C B:HIS201 4.7 9.2 1.0
CG B:HIS218 4.7 9.9 1.0
CG2 B:VAL273 4.7 10.4 1.0
C B:VAL273 4.9 8.8 1.0
ND1 B:HIS218 4.9 10.0 1.0
CA B:VAL273 5.0 8.4 1.0
C B:PHE200 5.0 9.3 1.0

Copper binding site 3 out of 6 in 1f1g

Go back to Copper Binding Sites List in 1f1g
Copper binding site 3 out of 6 in the Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu4005

b:13.1
occ:1.00
NE2 C:HIS358 2.0 9.4 1.0
ND1 C:HIS356 2.0 11.7 1.0
NE2 C:HIS430 2.0 10.1 1.0
CE1 C:HIS358 2.9 9.8 1.0
CD2 C:HIS430 3.0 10.4 1.0
CE1 C:HIS356 3.0 11.6 1.0
CD2 C:HIS358 3.0 9.2 1.0
CG C:HIS356 3.0 9.7 1.0
CE1 C:HIS430 3.1 10.5 1.0
CB C:HIS356 3.3 11.4 1.0
NE2 C:HIS373 3.3 11.4 1.0
CD2 C:HIS373 3.7 13.7 1.0
CB C:VAL428 3.9 9.5 1.0
O C:HOH3076 3.9 50.0 1.0
ND1 C:HIS358 4.1 9.9 1.0
CG1 C:VAL428 4.1 10.4 1.0
N C:HIS356 4.1 8.4 1.0
NE2 C:HIS356 4.1 11.0 1.0
CD2 C:HIS356 4.1 11.0 1.0
CG C:HIS430 4.1 10.2 1.0
ND1 C:HIS430 4.1 10.7 1.0
CG C:HIS358 4.1 8.6 1.0
CA C:HIS356 4.2 10.8 1.0
CE1 C:HIS373 4.2 10.4 1.0
O C:VAL428 4.3 9.3 1.0
O C:HIS356 4.6 9.9 1.0
C C:HIS356 4.6 9.0 1.0
CG C:HIS373 4.7 10.3 1.0
CG2 C:VAL428 4.7 10.4 1.0
C C:VAL428 4.9 8.7 1.0
ND1 C:HIS373 4.9 12.1 1.0
CA C:VAL428 4.9 8.8 1.0
C C:PHE355 5.0 8.8 1.0

Copper binding site 4 out of 6 in 1f1g

Go back to Copper Binding Sites List in 1f1g
Copper binding site 4 out of 6 in the Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu4007

b:13.1
occ:1.00
NE2 D:HIS513 1.9 10.3 1.0
ND1 D:HIS511 2.0 9.7 1.0
NE2 D:HIS585 2.0 9.2 1.0
CE1 D:HIS513 2.9 9.7 1.0
CE1 D:HIS511 2.9 10.1 1.0
CD2 D:HIS585 3.0 10.0 1.0
CD2 D:HIS513 3.0 9.2 1.0
CG D:HIS511 3.0 9.3 1.0
CE1 D:HIS585 3.1 10.6 1.0
CB D:HIS511 3.3 9.9 1.0
NE2 D:HIS528 3.3 11.8 1.0
CD2 D:HIS528 3.6 11.2 1.0
O D:HOH3080 3.8 50.0 1.0
O D:HOH3073 3.8 50.0 1.0
CB D:VAL583 3.9 9.0 1.0
ND1 D:HIS513 4.0 9.6 1.0
CD2 D:HIS511 4.1 10.7 1.0
NE2 D:HIS511 4.1 10.5 1.0
CG1 D:VAL583 4.1 10.4 1.0
CG D:HIS513 4.1 8.8 1.0
N D:HIS511 4.1 8.8 1.0
CG D:HIS585 4.1 9.9 1.0
ND1 D:HIS585 4.2 10.1 1.0
CE1 D:HIS528 4.2 11.3 1.0
CA D:HIS511 4.2 9.6 1.0
O D:VAL583 4.4 9.5 1.0
O D:HIS511 4.6 10.8 1.0
C D:HIS511 4.7 9.2 1.0
CG D:HIS528 4.7 9.8 1.0
CG2 D:VAL583 4.7 10.4 1.0
ND1 D:HIS528 4.9 9.8 1.0
C D:VAL583 4.9 8.8 1.0
CA D:VAL583 5.0 8.6 1.0
C D:PHE510 5.0 9.1 1.0

Copper binding site 5 out of 6 in 1f1g

Go back to Copper Binding Sites List in 1f1g
Copper binding site 5 out of 6 in the Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cu4009

b:13.1
occ:1.00
NE2 E:HIS668 2.0 9.1 1.0
NE2 E:HIS740 2.0 8.9 1.0
ND1 E:HIS666 2.0 10.9 1.0
CE1 E:HIS668 2.9 9.2 1.0
CD2 E:HIS740 3.0 9.3 1.0
CE1 E:HIS666 3.0 11.9 1.0
CD2 E:HIS668 3.0 8.3 1.0
CG E:HIS666 3.0 10.5 1.0
CE1 E:HIS740 3.0 10.2 1.0
CB E:HIS666 3.3 11.0 1.0
NE2 E:HIS683 3.3 11.3 1.0
CD2 E:HIS683 3.7 12.8 1.0
O E:HOH3082 3.8 50.0 1.0
CB E:VAL738 3.9 8.9 1.0
ND1 E:HIS668 4.1 9.4 1.0
CG1 E:VAL738 4.1 10.5 1.0
ND1 E:HIS740 4.1 10.8 1.0
NE2 E:HIS666 4.1 10.4 1.0
CG E:HIS740 4.1 9.1 1.0
N E:HIS666 4.1 8.8 1.0
CD2 E:HIS666 4.1 10.4 1.0
CG E:HIS668 4.1 8.8 1.0
CA E:HIS666 4.2 10.5 1.0
CE1 E:HIS683 4.2 10.7 1.0
O E:VAL738 4.4 8.5 1.0
O E:HIS666 4.6 10.2 1.0
C E:HIS666 4.6 8.8 1.0
CG E:HIS683 4.7 10.4 1.0
CG2 E:VAL738 4.8 10.4 1.0
C E:VAL738 4.9 8.1 1.0
ND1 E:HIS683 4.9 10.9 1.0
CA E:VAL738 5.0 7.9 1.0
C E:PHE665 5.0 9.4 1.0

Copper binding site 6 out of 6 in 1f1g

Go back to Copper Binding Sites List in 1f1g
Copper binding site 6 out of 6 in the Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure of Yeast Cuznsod Exposed to Nitric Oxide within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cu4011

b:12.9
occ:1.00
NE2 F:HIS823 1.9 8.5 1.0
ND1 F:HIS821 2.0 10.7 1.0
NE2 F:HIS895 2.0 9.3 1.0
CE1 F:HIS823 2.9 9.8 1.0
CD2 F:HIS895 3.0 9.5 1.0
CE1 F:HIS821 3.0 10.8 1.0
CD2 F:HIS823 3.0 8.1 1.0
CG F:HIS821 3.0 10.5 1.0
CE1 F:HIS895 3.0 10.5 1.0
CB F:HIS821 3.3 10.8 1.0
NE2 F:HIS838 3.3 11.2 1.0
CD2 F:HIS838 3.7 11.8 1.0
O F:HOH3078 3.8 50.0 1.0
O F:HOH3081 3.9 50.0 1.0
CB F:VAL893 3.9 9.3 1.0
ND1 F:HIS823 4.0 9.2 1.0
CG1 F:VAL893 4.1 10.2 1.0
CD2 F:HIS821 4.1 11.2 1.0
NE2 F:HIS821 4.1 10.7 1.0
CG F:HIS895 4.1 9.1 1.0
ND1 F:HIS895 4.1 10.3 1.0
CG F:HIS823 4.1 8.3 1.0
N F:HIS821 4.1 8.4 1.0
CE1 F:HIS838 4.2 10.4 1.0
CA F:HIS821 4.2 10.2 1.0
O F:VAL893 4.4 8.8 1.0
O F:HIS821 4.6 10.5 1.0
C F:HIS821 4.7 9.4 1.0
CG F:HIS838 4.7 10.5 1.0
CG2 F:VAL893 4.7 9.8 1.0
C F:VAL893 4.9 8.9 1.0
ND1 F:HIS838 4.9 10.5 1.0
CA F:VAL893 4.9 8.3 1.0
C F:PHE820 5.0 8.7 1.0

Reference:

P.J.Hart, M.M.Balbirnie, N.L.Ogihara, A.M.Nersissian, M.S.Weiss, J.S.Valentine, D.Eisenberg. A Structure-Based Mechanism For Copper-Zinc Superoxide Dismutase. Biochemistry V. 38 2167 1999.
ISSN: ISSN 0006-2960
PubMed: 10026301
DOI: 10.1021/BI982284U
Page generated: Sun Dec 13 10:58:47 2020

Last articles

Zn in 7O75
Zn in 7O73
Zn in 7O4I
Zn in 7O72
Zn in 7O4J
Zn in 7NVR
Zn in 7NVY
Zn in 7NVZ
Zn in 7NW0
Zn in 7O4K
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy