Zinc in PDB 1kfi: Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutase) From Paramecium

All present enzymatic activity of Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutase) From Paramecium:
5.4.2.2;

The structure of Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutase) From Paramecium, PDB code: 1kfi 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 (°)	67.346, 133.609, 150.545, 90.00, 90.00, 90.00
R / Rfree (%)	22.7 / 28.6

The binding sites of Zinc atom in the Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutase) From Paramecium (pdb code 1kfi). 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 of the Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutase) From Paramecium, PDB code: 1kfi:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutase) From Paramecium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutase) From Paramecium within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn700 b:21.7 occ:1.00 OD1 A:ASP312 1.9 30.8 1.0 O1 A:SO4601 1.9 38.6 1.0 OD2 A:ASP308 2.0 21.5 1.0 OD2 A:ASP310 2.0 19.6 1.0 CG A:ASP312 2.8 25.0 1.0 CG A:ASP310 2.9 16.7 1.0 CG A:ASP308 2.9 18.4 1.0 OD1 A:ASP310 3.1 12.8 1.0 S A:SO4601 3.1 50.1 1.0 OD1 A:ASP308 3.2 16.9 1.0 OD2 A:ASP312 3.3 19.4 1.0 O4 A:SO4601 3.5 52.0 1.0 O3 A:SO4601 3.7 44.5 1.0 CB A:SER126 3.8 49.7 1.0 CA A:SER126 4.0 46.0 1.0 N A:HIS127 4.1 45.7 1.0 CB A:ASP312 4.1 20.7 1.0 CG A:ARG313 4.2 17.1 1.0 N A:ASP312 4.2 19.9 1.0 CB A:ASP308 4.3 14.5 1.0 CB A:ASP310 4.3 14.3 1.0 O2 A:SO4601 4.3 41.5 1.0 C A:SER126 4.4 51.5 1.0 N A:ASP310 4.4 19.7 1.0 N A:ARG313 4.4 13.2 1.0 CA A:ASP312 4.5 21.0 1.0 C A:ASP312 4.7 20.1 1.0 CA A:ASP310 4.7 22.8 1.0 CD A:ARG313 4.7 15.6 1.0 CB A:HIS127 4.8 44.1 1.0 CB A:ARG313 4.8 11.8 1.0 C A:ASP310 4.9 21.3 1.0 NE A:ARG313 4.9 21.1 1.0 N A:ALA311 4.9 23.7 1.0 CA A:HIS127 5.0 40.9 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutase) From Paramecium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, PP63/Parafusin (Phosphoglucomutase) From Paramecium within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn700 b:33.6 occ:1.00 OD1 B:ASP308 1.8 25.6 1.0 OD1 B:ASP310 2.1 24.8 1.0 O2 B:SO4602 2.5 77.2 1.0 O1 B:SO4602 2.6 80.0 1.0 CB B:ASP312 2.6 27.1 1.0 CG B:ASP310 2.8 27.9 1.0 OD2 B:ASP310 2.9 18.0 1.0 CG B:ASP308 2.9 28.1 1.0 CG B:ASP312 2.9 31.0 1.0 S B:SO4602 3.1 73.5 1.0 OD1 B:ASP312 3.4 41.6 1.0 OD2 B:ASP308 3.4 32.5 1.0 OD2 B:ASP312 3.4 22.8 1.0 CA B:ASP312 3.8 27.5 1.0 O4 B:SO4602 4.0 77.3 1.0 CA B:SER126 4.1 47.9 1.0 O B:HOH770 4.1 44.3 1.0 N B:ASP312 4.1 28.1 1.0 CB B:ASP308 4.1 21.9 1.0 N B:ARG313 4.2 22.9 1.0 C B:SER126 4.2 49.7 1.0 O3 B:SO4602 4.2 71.9 1.0 CB B:ASP310 4.2 26.1 1.0 C B:ASP312 4.3 24.4 1.0 CG B:ARG313 4.3 21.1 1.0 N B:HIS127 4.4 46.9 1.0 CB B:SER126 4.5 50.7 1.0 N B:ASP310 4.5 30.8 1.0 O B:SER126 4.7 51.9 1.0 CA B:ASP310 4.7 30.2 1.0 C B:ASP310 4.8 30.4 1.0 CB B:ARG313 5.0 17.4 1.0

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