Iron 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:

Zinc (Zn) 2 atoms

Iron Binding Sites:

The binding sites of Iron 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 Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure Analysis of Catalytic Subunit of Human Calcineurin, PDB code: 5c1v:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5c1v

Go back to Iron Binding Sites List in 5c1v
Iron 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 Iron with other atoms in the Fe 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:Fe501

b:99.9
occ:1.00
O3 A:PO4503 1.5 92.5 1.0
OD2 A:ASP90 2.3 82.3 1.0
NE2 A:HIS92 2.5 77.3 1.0
OD2 A:ASP118 2.6 69.8 1.0
P A:PO4503 2.6 88.4 1.0
O4 A:PO4503 2.7 79.0 1.0
ZN A:ZN502 3.0 85.8 1.0
CE1 A:HIS92 3.1 77.6 1.0
CG A:ASP90 3.4 73.4 1.0
O2 A:PO4503 3.5 87.9 1.0
CG A:ASP118 3.7 70.6 1.0
CD2 A:HIS92 3.7 78.2 1.0
O A:HIS281 3.8 96.4 1.0
O1 A:PO4503 3.8 77.3 1.0
OD1 A:ASP90 3.9 72.1 1.0
CB A:ASP118 4.2 68.1 1.0
ND1 A:HIS281 4.2 96.9 1.0
NH2 A:ARG122 4.3 83.4 1.0
ND1 A:HIS92 4.4 75.2 1.0
OH A:TYR311 4.5 79.2 1.0
CA A:HIS281 4.5 88.3 1.0
C A:HIS281 4.6 90.9 1.0
CB A:ASP90 4.6 71.6 1.0
CD2 A:HIS151 4.6 82.2 1.0
NE2 A:HIS151 4.7 84.2 1.0
CG A:HIS92 4.7 76.2 1.0
OD1 A:ASP118 4.7 72.1 1.0
OD1 A:ASN150 4.8 80.4 1.0
NE2 A:HIS199 4.8 73.8 1.0
CE1 A:HIS199 4.9 71.5 1.0
CE1 A:PHE306 4.9 78.3 1.0
CE1 A:HIS281 5.0 0.1 1.0
NE A:ARG122 5.0 85.1 1.0

Iron binding site 2 out of 2 in 5c1v

Go back to Iron Binding Sites List in 5c1v
Iron 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 Iron with other atoms in the Fe 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:Fe501

b:99.9
occ:1.00
OD2 B:ASP90 2.4 0.2 1.0
O1 B:PO4503 2.4 99.9 1.0
NE2 B:HIS92 2.6 0.2 1.0
CD2 B:HIS92 3.2 0.7 1.0
CG B:ASP90 3.3 0.1 1.0
P B:PO4503 3.3 99.9 1.0
O4 B:PO4503 3.5 99.9 1.0
O3 B:PO4503 3.6 99.9 1.0
CE1 B:HIS92 3.7 0.8 1.0
O B:HIS281 3.8 0.2 1.0
CB B:ASP90 4.0 0.4 1.0
ZN B:ZN502 4.0 99.9 1.0
OD1 B:ASP90 4.1 0.5 1.0
OD2 B:ASP118 4.1 0.8 1.0
CG B:HIS92 4.5 0.1 1.0
C B:HIS281 4.7 0.1 1.0
ND1 B:HIS92 4.7 0.6 1.0
O2 B:PO4503 4.7 99.9 1.0
NH2 B:ARG122 4.8 0.5 1.0
CA B:HIS281 4.9 0.8 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: Mon Aug 5 20:48:04 2024

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