Calcium in PDB 1y1e: Human Formylglycine Generating Enzyme
Protein crystallography data
The structure of Human Formylglycine Generating Enzyme, PDB code: 1y1e
was solved by
M.G.Rudolph,
A.Dickmanns,
R.Ficner,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.80 /
1.73
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
61.956,
110.014,
43.474,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.4 /
24.2
|
Calcium Binding Sites:
The binding sites of Calcium atom in the Human Formylglycine Generating Enzyme
(pdb code 1y1e). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the
Human Formylglycine Generating Enzyme, PDB code: 1y1e:
Jump to Calcium binding site number:
1;
2;
Calcium binding site 1 out
of 2 in 1y1e
Go back to
Calcium Binding Sites List in 1y1e
Calcium binding site 1 out
of 2 in the Human Formylglycine Generating Enzyme
 Mono view
 Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of Human Formylglycine Generating Enzyme within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
X:Ca1001
b:21.7
occ:1.00
|
OE2
|
X:GLU130
|
2.3
|
21.0
|
1.0
|
O
|
X:ALA298
|
2.4
|
20.1
|
1.0
|
O
|
X:ASN293
|
2.4
|
21.9
|
1.0
|
O
|
X:HOH1007
|
2.4
|
20.5
|
1.0
|
O
|
X:GLY296
|
2.5
|
21.1
|
1.0
|
OE2
|
X:GLU300
|
2.5
|
24.7
|
1.0
|
CD
|
X:GLU130
|
3.3
|
22.5
|
1.0
|
CD
|
X:GLU300
|
3.4
|
21.9
|
1.0
|
C
|
X:ALA298
|
3.5
|
21.3
|
1.0
|
N
|
X:ALA298
|
3.6
|
21.6
|
1.0
|
C
|
X:ASN293
|
3.6
|
22.1
|
1.0
|
CG
|
X:GLU300
|
3.7
|
23.4
|
1.0
|
C
|
X:GLY296
|
3.7
|
21.2
|
1.0
|
CG
|
X:GLU130
|
3.9
|
19.5
|
1.0
|
CA
|
X:ALA298
|
4.0
|
21.2
|
1.0
|
O
|
X:ILE294
|
4.0
|
23.1
|
1.0
|
C
|
X:ILE294
|
4.2
|
22.8
|
1.0
|
O
|
X:GLY332
|
4.3
|
23.2
|
1.0
|
OE1
|
X:GLU130
|
4.3
|
21.7
|
1.0
|
CB
|
X:ASN297
|
4.3
|
22.5
|
1.0
|
CA
|
X:ILE294
|
4.4
|
22.8
|
1.0
|
N
|
X:GLY296
|
4.4
|
21.6
|
1.0
|
C
|
X:ASN297
|
4.4
|
21.5
|
1.0
|
N
|
X:ILE294
|
4.4
|
22.3
|
1.0
|
C
|
X:VAL295
|
4.4
|
22.3
|
1.0
|
CB
|
X:ASN293
|
4.4
|
21.3
|
1.0
|
OE1
|
X:GLU300
|
4.5
|
22.6
|
1.0
|
N
|
X:ASN297
|
4.5
|
21.0
|
1.0
|
NH2
|
X:ARG364
|
4.6
|
23.7
|
1.0
|
N
|
X:TRP299
|
4.6
|
21.9
|
1.0
|
CA
|
X:GLY296
|
4.6
|
21.2
|
1.0
|
CA
|
X:ASN293
|
4.6
|
21.5
|
1.0
|
CA
|
X:ASN297
|
4.6
|
21.9
|
1.0
|
CB
|
X:ALA298
|
4.6
|
21.4
|
1.0
|
O
|
X:VAL295
|
4.6
|
22.4
|
1.0
|
N
|
X:VAL295
|
4.7
|
23.1
|
1.0
|
CA
|
X:VAL295
|
4.9
|
22.7
|
1.0
|
C
|
X:TRP299
|
4.9
|
21.9
|
1.0
|
CA
|
X:TRP299
|
4.9
|
22.0
|
1.0
|
|
Calcium binding site 2 out
of 2 in 1y1e
Go back to
Calcium Binding Sites List in 1y1e
Calcium binding site 2 out
of 2 in the Human Formylglycine Generating Enzyme
 Mono view
 Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of Human Formylglycine Generating Enzyme within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
X:Ca1002
b:21.1
occ:1.00
|
O
|
X:ILE260
|
2.3
|
22.1
|
1.0
|
OD1
|
X:ASN259
|
2.3
|
22.4
|
1.0
|
O
|
X:PHE275
|
2.4
|
22.4
|
1.0
|
OD2
|
X:ASP273
|
2.4
|
23.6
|
1.0
|
OD1
|
X:ASP273
|
2.5
|
24.1
|
1.0
|
O
|
X:HOH1013
|
2.5
|
22.7
|
1.0
|
O
|
X:HOH1011
|
2.5
|
22.3
|
1.0
|
CG
|
X:ASP273
|
2.8
|
23.7
|
1.0
|
C
|
X:ILE260
|
3.5
|
22.4
|
1.0
|
C
|
X:PHE275
|
3.6
|
21.9
|
1.0
|
CG
|
X:ASN259
|
3.6
|
21.5
|
1.0
|
N
|
X:ILE260
|
3.8
|
21.5
|
1.0
|
OE1
|
X:GLN262
|
4.1
|
24.1
|
1.0
|
C
|
X:ASN259
|
4.2
|
20.4
|
1.0
|
CA
|
X:ILE260
|
4.2
|
22.0
|
1.0
|
CB
|
X:ASP273
|
4.3
|
23.4
|
1.0
|
CA
|
X:ASN259
|
4.3
|
20.8
|
1.0
|
CA
|
X:PHE275
|
4.4
|
21.9
|
1.0
|
N
|
X:PHE275
|
4.4
|
21.6
|
1.0
|
NE2
|
X:GLN262
|
4.4
|
23.5
|
1.0
|
CB
|
X:PHE275
|
4.4
|
21.4
|
1.0
|
ND2
|
X:ASN259
|
4.5
|
20.3
|
1.0
|
N
|
X:TRP261
|
4.5
|
22.4
|
1.0
|
CB
|
X:ASN259
|
4.5
|
20.9
|
1.0
|
N
|
X:GLN276
|
4.6
|
22.8
|
1.0
|
O
|
X:TYR334
|
4.6
|
24.6
|
1.0
|
OD1
|
X:ASN269
|
4.6
|
25.8
|
1.0
|
ND2
|
X:ASN269
|
4.6
|
20.8
|
1.0
|
CD
|
X:GLN262
|
4.6
|
24.1
|
1.0
|
CA
|
X:GLN276
|
4.7
|
23.4
|
1.0
|
O
|
X:GLN276
|
4.7
|
23.1
|
1.0
|
CA
|
X:TRP261
|
4.7
|
23.3
|
1.0
|
O
|
X:GLY277
|
4.9
|
22.6
|
1.0
|
C
|
X:GLN276
|
4.9
|
22.9
|
1.0
|
O
|
X:ASN259
|
4.9
|
19.6
|
1.0
|
CB
|
X:TYR334
|
4.9
|
24.3
|
1.0
|
|
Reference:
T.Dierks,
A.Dickmanns,
A.Preusser-Kunze,
B.Schmidt,
M.Mariappan,
K.Von Figura,
R.Ficner,
M.G.Rudolph.
Molecular Basis For Multiple Sulfatase Deficiency and Mechanism For Formylglycine Generation of the Human Formylglycine-Generating Enzyme. Cell(Cambridge,Mass.) V. 121 541 2005.
ISSN: ISSN 0092-8674
PubMed: 15907468
DOI: 10.1016/J.CELL.2005.03.001
Page generated: Fri Jul 12 07:51:31 2024
|