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Calcium in PDB 1z70: 1.15A Resolution Structure of the Formylglycine Generating Enzyme Fge

Protein crystallography data

The structure of 1.15A Resolution Structure of the Formylglycine Generating Enzyme Fge, PDB code: 1z70 was solved by M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.20 / 1.15
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 62.295, 109.765, 43.511, 90.00, 90.00, 90.00
R / Rfree (%) 13.8 / 17

Other elements in 1z70:

The structure of 1.15A Resolution Structure of the Formylglycine Generating Enzyme Fge also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the 1.15A Resolution Structure of the Formylglycine Generating Enzyme Fge (pdb code 1z70). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the 1.15A Resolution Structure of the Formylglycine Generating Enzyme Fge, PDB code: 1z70:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1z70

Go back to Calcium Binding Sites List in 1z70
Calcium binding site 1 out of 2 in the 1.15A Resolution Structure of the Formylglycine Generating Enzyme Fge


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of 1.15A Resolution Structure of the Formylglycine Generating Enzyme Fge within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Ca3001

b:6.4
occ:1.00
OE2 X:GLU1130 2.3 6.9 1.0
O X:ASN1293 2.3 6.7 1.0
OE2 X:GLU1300 2.4 7.1 1.0
O X:ALA1298 2.4 6.6 1.0
O X:HOH5002 2.4 7.3 1.0
O X:GLY1296 2.4 7.0 1.0
CD X:GLU1300 3.4 6.3 1.0
CD X:GLU1130 3.4 6.2 1.0
C X:ALA1298 3.5 6.7 1.0
C X:ASN1293 3.6 5.8 1.0
C X:GLY1296 3.6 6.8 1.0
CG X:GLU1300 3.6 7.4 1.0
N X:ALA1298 3.7 7.0 1.0
CG X:GLU1130 3.9 6.7 1.0
O X:ILE1294 3.9 7.6 1.0
C X:ILE1294 4.1 6.5 1.0
CA X:ALA1298 4.2 7.1 1.0
O X:GLY1332 4.3 7.9 1.0
CA X:ILE1294 4.3 6.4 1.0
CB X:ASN1297 4.4 6.7 1.0
N X:GLY1296 4.4 6.3 1.0
OE1 X:GLU1130 4.4 7.8 1.0
N X:ILE1294 4.4 6.2 1.0
CB X:ASN1293 4.4 5.6 1.0
C X:VAL1295 4.4 6.0 1.0
OE1 X:GLU1300 4.5 7.6 1.0
C X:ASN1297 4.5 6.8 1.0
NH2 X:ARG1364 4.5 6.5 1.0
N X:ASN1297 4.5 6.6 1.0
CA X:ASN1293 4.6 6.2 1.0
CA X:GLY1296 4.6 6.8 1.0
N X:TRP1299 4.6 6.5 1.0
CA X:ASN1297 4.6 6.7 1.0
O X:VAL1295 4.6 7.0 1.0
N X:VAL1295 4.7 6.8 1.0
CB X:ALA1298 4.7 8.6 1.0
CA X:VAL1295 4.8 6.8 1.0
C X:TRP1299 4.9 6.3 1.0
CA X:TRP1299 4.9 5.9 1.0

Calcium binding site 2 out of 2 in 1z70

Go back to Calcium Binding Sites List in 1z70
Calcium binding site 2 out of 2 in the 1.15A Resolution Structure of the Formylglycine Generating Enzyme Fge


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of 1.15A Resolution Structure of the Formylglycine Generating Enzyme Fge within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Ca3002

b:6.7
occ:1.00
OD1 X:ASN1259 2.3 7.0 1.0
O X:ILE1260 2.3 7.7 1.0
O X:PHE1275 2.4 8.4 1.0
O X:HOH5006 2.4 7.5 1.0
O X:HOH5004 2.4 7.4 1.0
OD1 X:ASP1273 2.5 7.3 1.0
OD2 X:ASP1273 2.5 7.5 1.0
CG X:ASP1273 2.8 7.0 1.0
C X:ILE1260 3.5 7.4 1.0
CG X:ASN1259 3.6 6.9 1.0
C X:PHE1275 3.6 7.4 1.0
N X:ILE1260 3.8 6.8 1.0
OE1 X:GLN1262 4.1 7.8 1.0
C X:ASN1259 4.2 6.0 1.0
CA X:ILE1260 4.3 7.0 1.0
CA X:ASN1259 4.3 6.5 1.0
CB X:ASP1273 4.3 7.7 1.0
CA X:PHE1275 4.4 6.8 1.0
N X:PHE1275 4.4 6.8 1.0
ND2 X:ASN1259 4.4 6.2 1.0
CB X:PHE1275 4.4 6.7 1.0
NE2 X:GLN1262 4.4 7.5 1.0
O X:TYR1334 4.5 7.6 1.0
CB X:ASN1259 4.5 7.3 1.0
N X:TRP1261 4.5 7.3 1.0
N X:GLN1276 4.5 7.8 1.0
O X:GLN1276 4.6 9.0 1.0
ND2 X:ASN1269 4.6 10.9 1.0
OD1 X:ASN1269 4.6 12.5 1.0
CD X:GLN1262 4.7 6.9 1.0
CA X:GLN1276 4.7 8.3 1.0
CA X:TRP1261 4.7 6.9 1.0
C X:GLN1276 4.8 7.9 1.0
O X:GLY1277 4.9 7.9 1.0
CB X:TYR1334 4.9 7.4 1.0
O X:ASN1259 5.0 6.9 1.0

Reference:

D.Roeser, A.Dickmanns, K.Gasow, M.G.Rudolph. De Novo Calcium/Sulfur Sad Phasing of the Human Formylglycine-Generating Enzyme Using in-House Data. Acta Crystallogr.,Sect.D V. 61 1057 2005.
ISSN: ISSN 0907-4449
PubMed: 16041070
DOI: 10.1107/S0907444905013831
Page generated: Sat Dec 12 03:29:50 2020

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