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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

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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

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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

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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

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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

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