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Zinc in PDB 1y75: A New Form of Catalytically Inactive Phospholipase A2 with An Unusual Disulphide Bridge Cys 32- Cys 49 Reveals Recognition For N- Acetylglucosmine

Enzymatic activity of A New Form of Catalytically Inactive Phospholipase A2 with An Unusual Disulphide Bridge Cys 32- Cys 49 Reveals Recognition For N- Acetylglucosmine

All present enzymatic activity of A New Form of Catalytically Inactive Phospholipase A2 with An Unusual Disulphide Bridge Cys 32- Cys 49 Reveals Recognition For N- Acetylglucosmine:
3.1.1.4;

Protein crystallography data

The structure of A New Form of Catalytically Inactive Phospholipase A2 with An Unusual Disulphide Bridge Cys 32- Cys 49 Reveals Recognition For N- Acetylglucosmine, PDB code: 1y75 was solved by T.Jabeen, N.Singh, J.Jasti, R.K.Singh, S.Sharma, M.Perbandt, C.Betzel, P.Kaur, A.Srinivasan, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.95 / 2.30
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 77.656, 77.656, 68.424, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 25.6

Zinc Binding Sites:

The binding sites of Zinc atom in the A New Form of Catalytically Inactive Phospholipase A2 with An Unusual Disulphide Bridge Cys 32- Cys 49 Reveals Recognition For N- Acetylglucosmine (pdb code 1y75). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the A New Form of Catalytically Inactive Phospholipase A2 with An Unusual Disulphide Bridge Cys 32- Cys 49 Reveals Recognition For N- Acetylglucosmine, PDB code: 1y75:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1y75

Go back to Zinc Binding Sites List in 1y75
Zinc binding site 1 out of 2 in the A New Form of Catalytically Inactive Phospholipase A2 with An Unusual Disulphide Bridge Cys 32- Cys 49 Reveals Recognition For N- Acetylglucosmine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of A New Form of Catalytically Inactive Phospholipase A2 with An Unusual Disulphide Bridge Cys 32- Cys 49 Reveals Recognition For N- Acetylglucosmine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:40.9
occ:1.00
 OD2 A:ASP24 2.1 45.5 1.0
OD2 B:ASP24 2.2 43.1 1.0
OD1 A:ASN112 2.6 42.5 1.0
OD1 B:ASP24 2.6 50.1 1.0
OD1 A:ASP24 2.6 45.9 1.0
CG A:ASP24 2.7 43.7 1.0
CG B:ASP24 2.7 47.2 1.0
ND2 B:ASN112 3.4 55.2 1.0
CG A:ASN112 3.8 42.0 1.0
CA B:ASN112 4.1 53.1 1.0
CA A:ASN112 4.1 40.8 1.0
CB B:ASP24 4.2 44.9 1.0
CB A:ASP24 4.2 41.3 1.0
O B:ILE113 4.3 50.9 1.0
O A:ILE113 4.3 37.1 1.0
O B:HOH201 4.4 48.4 1.0
C B:ASN112 4.4 52.1 1.0
CB A:ASN112 4.4 42.5 1.0
C A:ASN112 4.5 39.5 1.0
CG B:ASN112 4.6 54.8 1.0
O A:HOH406 4.6 19.1 1.0
O B:ASN112 4.7 51.0 1.0
ND2 A:ASN112 4.8 40.4 1.0
N B:ILE113 4.8 51.0 1.0
O A:ASN112 4.9 39.1 1.0
CB B:ASN112 5.0 53.9 1.0

Zinc binding site 2 out of 2 in 1y75

Go back to Zinc Binding Sites List in 1y75
Zinc binding site 2 out of 2 in the A New Form of Catalytically Inactive Phospholipase A2 with An Unusual Disulphide Bridge Cys 32- Cys 49 Reveals Recognition For N- Acetylglucosmine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of A New Form of Catalytically Inactive Phospholipase A2 with An Unusual Disulphide Bridge Cys 32- Cys 49 Reveals Recognition For N- Acetylglucosmine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:53.4
occ:0.50
 OE1 A:GLU71 2.1 48.1 1.0
CD A:GLU71 2.6 48.4 1.0
OE2 A:GLU71 2.7 48.0 1.0
CG A:GLU71 4.0 48.4 1.0
O A:HOH502 4.0 62.8 1.0
OG A:SER73 4.7 61.8 1.0
CB A:GLU71 5.0 44.2 1.0

Reference:

T.Jabeen, N.Singh, R.K.Singh, J.Jasti, S.Sharma, P.Kaur, A.Srinivasan, T.P.Singh. Crystal Structure of A Heterodimer of Phospholipase A2 From Naja Naja Sagittifera at 2.3 A Resolution Reveals the Presence of A New PLA2-Like Protein with A Novel Cys 32-Cys 49 Disulphide Bridge with A Bound Sugar at the Substrate-Binding Site Proteins V. 62 329 2006.
ISSN: ISSN 0887-3585
PubMed: 16287060
DOI: 10.1002/PROT.20708
Page generated: Wed Oct 16 20:46:12 2024

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