Atomistry » Zinc » PDB 3e2d-3eb5 » 3ea2
Atomistry »
  Zinc »
    PDB 3e2d-3eb5 »
      3ea2 »

Zinc in PDB 3ea2: Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis

Enzymatic activity of Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis

All present enzymatic activity of Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis:
4.6.1.13;

Protein crystallography data

The structure of Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis, PDB code: 3ea2 was solved by X.Shi, C.Shao, X.Zhang, C.Zambonelli, A.G.Redfied, J.F.Head, B.A.Seaton, M.F.Roberts, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.518, 97.226, 112.727, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 22.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis (pdb code 3ea2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis, PDB code: 3ea2:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 3ea2

Go back to Zinc Binding Sites List in 3ea2
Zinc binding site 1 out of 6 in the Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis


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 Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:24.6
occ:1.00
 OD2 A:ASP224 1.9 20.9 1.0
ND1 A:HIS227 2.2 21.8 1.0
O A:HOH920 2.2 22.4 1.0
O A:HOH1045 2.3 26.1 1.0
O A:HOH1070 2.4 31.9 1.0
O A:HOH915 2.4 25.1 1.0
CG A:ASP224 2.9 20.7 1.0
CG A:HIS227 3.2 22.4 1.0
CE1 A:HIS227 3.2 22.9 1.0
OD1 A:ASP224 3.3 18.7 1.0
CB A:HIS227 3.4 22.5 1.0
ND2 A:ASN221 4.0 20.1 1.0
CB A:ASN193 4.1 23.0 1.0
CB A:ASP224 4.2 21.9 1.0
O A:HOH958 4.2 29.6 1.0
O A:HOH1106 4.2 33.6 1.0
OD1 A:ASN193 4.2 24.1 1.0
O A:HOH1082 4.3 43.5 1.0
CD2 A:HIS227 4.3 23.8 1.0
NE2 A:HIS227 4.3 22.9 1.0
CG A:ASN193 4.4 25.5 1.0
CA A:HIS227 4.4 20.9 1.0
ND2 A:ASN226 4.8 29.2 1.0
O A:HOH1145 4.9 35.0 1.0
N A:HIS227 4.9 22.3 1.0

Zinc binding site 2 out of 6 in 3ea2

Go back to Zinc Binding Sites List in 3ea2
Zinc binding site 2 out of 6 in the Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis


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 Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn902

b:23.5
occ:1.00
 OE2 A:GLU278 1.6 27.4 1.0
CD A:GLU278 2.0 28.4 1.0
NE2 A:HIS61 2.1 16.0 1.0
OE1 A:GLU278 2.2 24.5 1.0
CE1 A:HIS61 3.0 17.6 1.0
CD2 A:HIS61 3.2 17.4 1.0
CG A:GLU278 3.3 24.3 1.0
O A:HOH906 3.4 4.8 1.0
OH A:TYR57 3.7 17.3 1.0
O A:HOH1154 3.8 23.9 1.0
CE2 A:TYR57 4.1 18.8 1.0
CZ A:TYR57 4.1 16.0 1.0
ND1 A:HIS61 4.1 16.0 1.0
CG A:HIS61 4.3 17.7 1.0
O A:HOH1221 4.4 35.3 1.0
O A:HOH1201 4.4 22.1 1.0
CB A:GLU278 4.4 22.7 1.0
O A:HOH1035 4.5 27.5 1.0
O A:HOH1150 4.6 42.6 1.0

Zinc binding site 3 out of 6 in 3ea2

Go back to Zinc Binding Sites List in 3ea2
Zinc binding site 3 out of 6 in the Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn903

b:84.5
occ:1.00
 OE2 A:GLU93 2.4 18.7 1.0
O A:HOH1061 2.7 16.1 1.0
O A:HOH1083 2.7 26.9 1.0
CD A:GLU93 3.4 18.7 1.0
CG A:GLU93 3.7 18.0 1.0
CE A:LYS38 4.2 12.6 1.0
NZ A:LYS38 4.2 13.6 1.0
CZ A:PHE37 4.3 15.3 1.0
CE2 A:PHE37 4.3 14.0 1.0
O A:HOH1239 4.5 45.2 1.0
OE1 A:GLU93 4.5 20.2 1.0
CB A:ASP54 4.6 19.2 1.0
CG A:GLU97 4.7 19.6 1.0
CD2 A:PHE55 4.9 12.2 1.0
CD A:GLU97 5.0 24.0 1.0

Zinc binding site 4 out of 6 in 3ea2

Go back to Zinc Binding Sites List in 3ea2
Zinc binding site 4 out of 6 in the Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn905

b:21.0
occ:1.00
 O A:HOH1011 2.1 18.9 1.0
OD2 A:ASP75 2.1 17.2 1.0
OD2 A:ASP74 2.1 20.0 1.0
O A:HOH1057 2.1 18.9 1.0
CG A:ASP75 2.9 17.9 1.0
CG A:ASP74 2.9 19.9 1.0
OD1 A:ASP74 3.1 19.6 1.0
OD1 A:ASP75 3.2 19.4 1.0
O A:HOH1064 3.7 23.8 1.0
O A:HOH909 4.1 14.8 1.0
CB A:ASP75 4.3 17.9 1.0
CB A:ASP74 4.3 17.7 1.0
N A:ASP75 4.4 17.5 1.0
O A:HOH1130 4.4 40.6 1.0
C A:ASP74 4.6 17.2 1.0
CA A:ASP75 4.6 16.7 1.0
O A:ASP74 5.0 16.4 1.0

Zinc binding site 5 out of 6 in 3ea2

Go back to Zinc Binding Sites List in 3ea2
Zinc binding site 5 out of 6 in the Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn904

b:54.8
occ:1.00
 OE2 B:GLU278 1.8 18.4 1.0
NE2 B:HIS61 2.3 12.3 1.0
CE1 B:HIS61 2.8 13.4 1.0
CD B:GLU278 2.9 18.4 1.0
O B:HOH1066 3.3 37.1 1.0
OH B:TYR57 3.4 17.1 1.0
CG B:GLU278 3.4 17.6 1.0
CD2 B:HIS61 3.5 12.8 1.0
CE2 B:TYR57 3.7 14.3 1.0
CZ B:TYR57 3.8 15.7 1.0
OE1 B:GLU278 4.0 16.2 1.0
ND1 B:HIS61 4.1 12.6 1.0
CB B:GLU278 4.4 16.2 1.0
CG B:HIS61 4.4 14.3 1.0
CD2 B:TYR57 4.7 11.6 1.0
CE1 B:TYR57 5.0 13.1 1.0

Zinc binding site 6 out of 6 in 3ea2

Go back to Zinc Binding Sites List in 3ea2
Zinc binding site 6 out of 6 in the Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of the Myo-Inositol Bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn906

b:30.2
occ:1.00
 OD2 B:ASP224 1.9 29.1 1.0
O B:HOH952 2.2 28.7 1.0
ND1 B:HIS227 2.2 25.5 1.0
O B:HOH921 2.3 24.1 1.0
O B:HOH1067 2.4 33.7 1.0
O B:HOH1042 2.5 31.9 1.0
CG B:ASP224 3.0 28.3 1.0
CG B:HIS227 3.1 26.0 1.0
CE1 B:HIS227 3.3 25.5 1.0
CB B:HIS227 3.3 25.3 1.0
OD1 B:ASP224 3.4 28.0 1.0
ND2 B:ASN221 4.1 25.0 1.0
CB B:ASN193 4.1 29.9 1.0
CG B:ASN193 4.2 30.5 1.0
CB B:ASP224 4.2 28.5 1.0
CD2 B:HIS227 4.3 25.9 1.0
CA B:HIS227 4.3 24.0 1.0
NE2 B:HIS227 4.3 26.2 1.0
OD1 B:ASN193 4.4 29.9 1.0
O B:HOH1132 4.7 43.6 1.0
ND2 B:ASN193 4.7 28.6 1.0
N B:HIS227 4.8 25.0 1.0
OD1 B:ASN226 4.8 34.5 1.0

Reference:

X.Shi, C.Shao, X.Zhang, C.Zambonelli, A.G.Redfield, J.F.Head, B.A.Seaton, M.F.Roberts. Modulation of Bacillus Thuringiensis Phosphatidylinositol-Specific Phospholipase C Activity By Mutations in the Putative Dimerization Interface. J.Biol.Chem. V. 284 15607 2009.
ISSN: ISSN 0021-9258
PubMed: 19369255
DOI: 10.1074/JBC.M901601200
Page generated: Thu Oct 24 12:41:29 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy