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Zinc in PDB 5c1v: Crystal Structure Analysis of Catalytic Subunit of Human Calcineurin

Enzymatic activity of Crystal Structure Analysis of Catalytic Subunit of Human Calcineurin

All present enzymatic activity of Crystal Structure Analysis of Catalytic Subunit of Human Calcineurin:
3.1.3.16;

Protein crystallography data

The structure of Crystal Structure Analysis of Catalytic Subunit of Human Calcineurin, PDB code: 5c1v was solved by A.Guasch, I.Fita, R.Perez-Luque, D.Aparicio, A.Aranguren-Ibanez, M.Perez-Riba, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.80 / 3.35
Space group P 62 2 2
Cell size a, b, c (Å), α, β, γ (°) 185.008, 185.008, 106.744, 90.00, 90.00, 120.00
R / Rfree (%) 21.6 / 24.9

Other elements in 5c1v:

The structure of Crystal Structure Analysis of Catalytic Subunit of Human Calcineurin also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure Analysis of Catalytic Subunit of Human Calcineurin (pdb code 5c1v). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure Analysis of Catalytic Subunit of Human Calcineurin, PDB code: 5c1v:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5c1v

Go back to Zinc Binding Sites List in 5c1v
Zinc binding site 1 out of 2 in the Crystal Structure Analysis of Catalytic Subunit of Human Calcineurin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure Analysis of Catalytic Subunit of Human Calcineurin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn502

b:85.8
occ:1.00
O4 A:PO4503 1.8 79.0 1.0
OD1 A:ASN150 2.0 80.4 1.0
OD2 A:ASP118 2.1 69.8 1.0
ND1 A:HIS281 2.3 96.9 1.0
NE2 A:HIS199 2.4 73.8 1.0
CE1 A:HIS281 2.8 0.1 1.0
CG A:ASN150 2.9 95.2 1.0
FE A:FE501 3.0 99.9 1.0
ND2 A:ASN150 3.1 0.8 1.0
CG A:ASP118 3.1 70.6 1.0
CE1 A:HIS199 3.1 71.5 1.0
P A:PO4503 3.2 88.4 1.0
CG A:HIS281 3.3 99.5 1.0
CD2 A:HIS199 3.4 72.4 1.0
OD1 A:ASP118 3.5 72.1 1.0
O3 A:PO4503 3.5 92.5 1.0
CA A:HIS281 3.7 88.3 1.0
NE2 A:HIS281 3.9 0.6 1.0
CB A:HIS281 3.9 97.5 1.0
CD2 A:HIS281 4.1 99.0 1.0
OD2 A:ASP90 4.1 82.3 1.0
O1 A:PO4503 4.2 77.3 1.0
O2 A:PO4503 4.2 87.9 1.0
ND1 A:HIS199 4.3 66.9 1.0
CB A:ASN150 4.4 86.9 1.0
OD1 A:ASP90 4.4 72.1 1.0
O A:HIS281 4.4 96.4 1.0
CB A:ASP118 4.4 68.1 1.0
CG A:HIS199 4.4 69.8 1.0
C A:HIS281 4.6 90.9 1.0
N A:ASN150 4.6 77.4 1.0
CD2 A:HIS151 4.6 82.2 1.0
N A:HIS281 4.7 83.9 1.0
CG A:ASP90 4.7 73.4 1.0
O A:LEU231 4.9 76.2 1.0
CA A:ASN150 5.0 77.9 1.0

Zinc binding site 2 out of 2 in 5c1v

Go back to Zinc Binding Sites List in 5c1v
Zinc binding site 2 out of 2 in the Crystal Structure Analysis of Catalytic Subunit of Human Calcineurin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure Analysis of Catalytic Subunit of Human Calcineurin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn502

b:99.9
occ:1.00
OD2 B:ASP118 1.5 0.8 1.0
O4 B:PO4503 1.9 99.9 1.0
NE2 B:HIS199 2.6 0.5 1.0
OD1 B:ASN150 2.7 0.1 1.0
CG B:ASP118 2.7 0.4 1.0
ND1 B:HIS281 2.9 0.2 1.0
P B:PO4503 2.9 99.9 1.0
CE1 B:HIS199 3.0 0.3 1.0
O1 B:PO4503 3.2 99.9 1.0
OD1 B:ASP118 3.3 0.4 1.0
OD2 B:ASP90 3.4 0.2 1.0
O2 B:PO4503 3.5 99.9 1.0
CG B:ASN150 3.5 0.4 1.0
CE1 B:HIS281 3.5 0.5 1.0
ND2 B:ASN150 3.7 0.2 1.0
OD1 B:ASP90 3.8 0.5 1.0
CB B:ASP118 3.8 0.2 1.0
CA B:HIS281 3.9 0.8 1.0
CG B:HIS281 3.9 0.9 1.0
CD2 B:HIS199 3.9 0.6 1.0
CG B:ASP90 4.0 0.1 1.0
FE B:FE501 4.0 99.9 1.0
O3 B:PO4503 4.2 99.9 1.0
CB B:HIS281 4.3 0.0 1.0
ND1 B:HIS199 4.3 1.0 1.0
NE2 B:HIS92 4.4 0.2 1.0
CD2 B:HIS151 4.5 0.5 1.0
O B:HIS281 4.5 0.2 1.0
CE1 B:HIS92 4.5 0.8 1.0
N B:HIS281 4.6 0.6 1.0
NE2 B:HIS281 4.7 0.7 1.0
CG B:HIS199 4.7 0.6 1.0
C B:HIS281 4.7 0.1 1.0
CD2 B:HIS281 4.8 0.1 1.0
N B:ASN150 4.9 0.4 1.0
CB B:ASN150 5.0 1.0 1.0

Reference:

A.Guasch, A.Aranguren-Ibanez, R.Perez-Luque, D.Aparicio, S.Martinez-Hyer, M.C.Mulero, E.Serrano-Candelas, M.Perez-Riba, I.Fita. Calcineurin Undergoes A Conformational Switch Evoked Via Peptidyl-Prolyl Isomerization. Plos One V. 10 34569 2015.
ISSN: ESSN 1932-6203
PubMed: 26248042
DOI: 10.1371/JOURNAL.PONE.0134569
Page generated: Sun Oct 27 13:39:34 2024

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