Atomistry » Manganese » PDB 3cev-3ea3 » 3ea3
Atomistry »
  Manganese »
    PDB 3cev-3ea3 »
      3ea3 »

Manganese in PDB 3ea3: Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis

Enzymatic activity of Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis

All present enzymatic activity of Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis:
4.6.1.13;

Protein crystallography data

The structure of Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis, PDB code: 3ea3 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 / 1.78
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 47.666, 56.352, 59.852, 92.36, 99.38, 113.21
R / Rfree (%) 18.5 / 22.1

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis (pdb code 3ea3). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 5 binding sites of Manganese where determined in the Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis, PDB code: 3ea3:
Jump to Manganese binding site number: 1; 2; 3; 4; 5;

Manganese binding site 1 out of 5 in 3ea3

Go back to Manganese Binding Sites List in 3ea3
Manganese binding site 1 out of 5 in the Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn299

b:22.1
occ:1.00
 O A:HOH564 2.0 23.2 1.0
O A:HOH507 2.2 25.6 1.0
O A:HOH306 2.2 20.5 1.0
O A:HOH553 2.2 15.3 1.0
OD2 A:ASP33 2.3 22.3 1.0
NE2 A:HIS82 2.4 23.3 1.0
CD2 A:HIS82 3.0 22.5 1.0
CG A:ASP33 3.2 21.4 1.0
CE1 A:HIS82 3.4 21.8 1.0
OD1 A:ASP33 3.5 24.4 1.0
CE1 A:HIS32 3.8 15.9 1.0
NE2 A:HIS32 3.8 15.6 1.0
O A:HOH511 4.1 32.4 1.0
CG A:HIS82 4.2 20.7 1.0
O A:HOH430 4.3 21.4 1.0
ND1 A:HIS82 4.4 21.6 1.0
O A:HOH388 4.4 36.4 1.0
NH1 A:ARG69 4.4 26.9 1.0
CB A:ASP33 4.6 17.4 1.0
OE2 A:GLU117 4.6 20.1 1.0
NH2 A:ARG69 4.9 22.6 1.0
CZ A:ARG69 4.9 22.9 1.0
ND1 A:HIS32 5.0 15.3 1.0

Manganese binding site 2 out of 5 in 3ea3

Go back to Manganese Binding Sites List in 3ea3
Manganese binding site 2 out of 5 in the Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn300

b:30.2
occ:1.00
 OD2 A:ASP224 2.1 28.1 1.0
O A:HOH554 2.2 28.3 1.0
O A:HOH558 2.4 32.5 1.0
O A:HOH557 2.4 28.5 1.0
ND1 A:HIS227 2.4 26.1 1.0
CG A:ASP224 3.1 29.2 1.0
CG A:HIS227 3.4 25.0 1.0
CE1 A:HIS227 3.4 24.4 1.0
OD1 A:ASP224 3.5 30.0 1.0
CB A:HIS227 3.6 25.2 1.0
OD1 A:ASN193 3.7 35.8 1.0
ND2 A:ASN221 4.1 31.0 1.0
CB A:ASP224 4.4 28.7 1.0
CB A:ASN193 4.4 30.6 1.0
NE2 A:HIS227 4.5 25.1 1.0
CG A:ASN193 4.5 34.0 1.0
CD2 A:HIS227 4.5 25.4 1.0
CA A:HIS227 4.7 23.8 1.0
O A:HOH505 4.9 37.5 1.0

Manganese binding site 3 out of 5 in 3ea3

Go back to Manganese Binding Sites List in 3ea3
Manganese binding site 3 out of 5 in the Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn301

b:36.2
occ:1.00
 O A:HOH468 1.9 22.2 1.0
OD2 A:ASP54 2.0 22.4 1.0
CG A:ASP54 2.9 20.4 1.0
OD1 A:ASP54 3.1 17.4 1.0
CB A:ASP54 4.3 18.9 1.0
O A:HOH378 4.4 31.0 1.0

Manganese binding site 4 out of 5 in 3ea3

Go back to Manganese Binding Sites List in 3ea3
Manganese binding site 4 out of 5 in the Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn299

b:21.4
occ:1.00
 O B:HOH730 2.1 25.8 1.0
O B:HOH729 2.3 24.8 1.0
OD2 B:ASP33 2.3 19.8 1.0
O B:HOH728 2.3 21.3 1.0
O B:HOH727 2.4 22.7 1.0
NE2 B:HIS82 2.4 19.8 1.0
CD2 B:HIS82 3.1 18.2 1.0
CG B:ASP33 3.2 17.1 1.0
OD1 B:ASP33 3.4 17.6 1.0
CE1 B:HIS82 3.5 19.9 1.0
NE2 B:HIS32 3.8 16.0 1.0
CE1 B:HIS32 4.0 19.4 1.0
O B:HOH623 4.2 21.8 1.0
O B:HOH674 4.3 34.1 1.0
CG B:HIS82 4.3 18.5 1.0
NH1 B:ARG69 4.3 26.4 1.0
ND1 B:HIS82 4.4 19.1 1.0
OE2 B:GLU117 4.5 21.4 1.0
CB B:ASP33 4.6 14.8 1.0
CZ B:ARG69 4.9 23.7 1.0
NH2 B:ARG69 5.0 23.0 1.0

Manganese binding site 5 out of 5 in 3ea3

Go back to Manganese Binding Sites List in 3ea3
Manganese binding site 5 out of 5 in the Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Crystal Structure of the Y246S/Y247S/Y248S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C From Bacillus Thuringiensis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn300

b:31.5
occ:1.00
 OD2 B:ASP224 2.1 28.1 1.0
O B:HOH736 2.1 30.8 1.0
O B:HOH508 2.1 30.6 1.0
O B:HOH732 2.2 42.8 1.0
O B:HOH569 2.3 30.7 1.0
ND1 B:HIS227 2.4 23.8 1.0
CG B:ASP224 3.1 26.8 1.0
CE1 B:HIS227 3.3 23.6 1.0
CG B:HIS227 3.4 24.4 1.0
OD1 B:ASP224 3.6 27.2 1.0
CB B:HIS227 3.6 23.6 1.0
OD1 B:ASN193 4.0 30.2 1.0
CB B:ASN193 4.2 28.1 1.0
CG B:ASN193 4.2 29.9 1.0
ND2 B:ASN221 4.3 27.6 1.0
O B:HOH578 4.3 31.6 1.0
CB B:ASP224 4.4 28.4 1.0
OD1 B:ASN226 4.4 37.5 1.0
O B:HOH735 4.4 36.4 1.0
NE2 B:HIS227 4.4 24.1 1.0
CD2 B:HIS227 4.5 23.7 1.0
O B:HOH651 4.6 36.7 1.0
CA B:HIS227 4.7 23.4 1.0
O B:HOH605 4.9 43.9 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: Sat Oct 5 16:10:44 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy