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Calcium in PDB 1kfq: Crystal Structure of Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutse) From Paramecium. Open Form

Enzymatic activity of Crystal Structure of Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutse) From Paramecium. Open Form

All present enzymatic activity of Crystal Structure of Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutse) From Paramecium. Open Form:
5.4.2.2;

Protein crystallography data

The structure of Crystal Structure of Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutse) From Paramecium. Open Form, PDB code: 1kfq was solved by S.Mueller, K.Diederichs, J.Breed, R.Kissmehl, K.Hauser, H.Plattner, W.Welte, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 64.900, 90.600, 212.000, 90.00, 90.00, 90.00
R / Rfree (%) 23.3 / 28.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutse) From Paramecium. Open Form (pdb code 1kfq). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutse) From Paramecium. Open Form, PDB code: 1kfq:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1kfq

Go back to Calcium Binding Sites List in 1kfq
Calcium binding site 1 out of 2 in the Crystal Structure of Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutse) From Paramecium. Open Form


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutse) From Paramecium. Open Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca700

b:41.6
occ:1.00
OG A:SER126 2.1 41.2 1.0
OD1 A:ASP308 2.4 20.8 1.0
OD2 A:ASP310 2.5 40.7 1.0
CB A:ASP312 2.6 23.5 1.0
OD1 A:ASP312 3.0 40.8 1.0
CG A:ASP312 3.2 35.5 1.0
CG A:ASP310 3.3 32.7 1.0
CB A:SER126 3.3 31.6 1.0
OD1 A:ASP310 3.3 31.9 1.0
CG A:ASP308 3.4 12.1 1.0
OD2 A:ASP308 3.8 24.7 1.0
CA A:SER126 3.9 30.2 1.0
CA A:ASP312 4.0 20.5 1.0
N A:ASP312 4.4 20.3 1.0
N A:ARG313 4.4 18.1 1.0
OD2 A:ASP312 4.4 44.6 1.0
C A:SER126 4.5 28.8 1.0
CG A:ARG313 4.5 16.6 1.0
N A:HIS127 4.5 25.2 1.0
CD2 A:HIS127 4.6 35.3 1.0
CB A:ASP308 4.7 8.2 1.0
C A:ASP312 4.7 18.5 1.0
CB A:ASP310 4.7 19.9 1.0
CD A:ARG313 5.0 15.1 1.0

Calcium binding site 2 out of 2 in 1kfq

Go back to Calcium Binding Sites List in 1kfq
Calcium binding site 2 out of 2 in the Crystal Structure of Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutse) From Paramecium. Open Form


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutse) From Paramecium. Open Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca700

b:39.1
occ:1.00
OG B:SER126 2.1 37.6 1.0
OD2 B:ASP310 2.5 43.2 1.0
OD1 B:ASP308 2.5 18.2 1.0
CB B:ASP312 3.1 22.1 1.0
CG B:ASP312 3.2 35.5 1.0
CB B:SER126 3.2 28.4 1.0
CG B:ASP308 3.3 10.8 1.0
OD1 B:ASP312 3.3 46.0 1.0
CG B:ASP310 3.3 35.8 1.0
OD1 B:ASP310 3.4 36.0 1.0
CA B:SER126 3.7 27.5 1.0
OD2 B:ASP308 3.7 21.4 1.0
OD2 B:ASP312 3.8 38.4 1.0
C B:SER126 4.1 28.1 1.0
N B:HIS127 4.2 24.2 1.0
CA B:ASP312 4.3 17.9 1.0
N B:ASP312 4.4 14.6 1.0
CB B:ASP308 4.4 9.4 1.0
CD2 B:HIS127 4.4 33.1 1.0
N B:ARG313 4.6 16.6 1.0
CG B:ARG313 4.7 17.9 1.0
CB B:ASP310 4.7 23.4 1.0
O B:SER126 4.9 30.0 1.0
N B:ASP310 4.9 16.3 1.0
N B:SER126 5.0 28.2 1.0

Reference:

S.Muller, K.Diederichs, J.Breed, R.Kissmehl, K.Hauser, H.Plattner, W.Welte. Crystal Structure Analysis of the Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutase), From Paramecium Reveals Significant Conformational Variability. J.Mol.Biol. V. 315 141 2002.
ISSN: ISSN 0022-2836
PubMed: 11779235
DOI: 10.1006/JMBI.2001.5168
Page generated: Sat Dec 12 03:03:44 2020

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