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Calcium in PDB 3bp2: Role of the N-Terminus in the Interaction of Pancreatic Phospholipase A2 with Aggregated Substrates. Properties and Crystal Structure of Transaminated Phospholipase A2

Enzymatic activity of Role of the N-Terminus in the Interaction of Pancreatic Phospholipase A2 with Aggregated Substrates. Properties and Crystal Structure of Transaminated Phospholipase A2

All present enzymatic activity of Role of the N-Terminus in the Interaction of Pancreatic Phospholipase A2 with Aggregated Substrates. Properties and Crystal Structure of Transaminated Phospholipase A2:
3.1.1.4;

Protein crystallography data

The structure of Role of the N-Terminus in the Interaction of Pancreatic Phospholipase A2 with Aggregated Substrates. Properties and Crystal Structure of Transaminated Phospholipase A2, PDB code: 3bp2 was solved by B.W.Dijkstra, J.Drenth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.680, 64.850, 37.910, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Role of the N-Terminus in the Interaction of Pancreatic Phospholipase A2 with Aggregated Substrates. Properties and Crystal Structure of Transaminated Phospholipase A2 (pdb code 3bp2). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Role of the N-Terminus in the Interaction of Pancreatic Phospholipase A2 with Aggregated Substrates. Properties and Crystal Structure of Transaminated Phospholipase A2, PDB code: 3bp2:

Calcium binding site 1 out of 1 in 3bp2

Go back to Calcium Binding Sites List in 3bp2
Calcium binding site 1 out of 1 in the Role of the N-Terminus in the Interaction of Pancreatic Phospholipase A2 with Aggregated Substrates. Properties and Crystal Structure of Transaminated Phospholipase A2


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Role of the N-Terminus in the Interaction of Pancreatic Phospholipase A2 with Aggregated Substrates. Properties and Crystal Structure of Transaminated Phospholipase A2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca124

b:13.0
occ:1.00
 O A:TYR28 2.1 7.9 1.0
OD2 A:ASP49 2.2 4.9 1.0
OD1 A:ASP49 2.3 5.1 1.0
O A:GLY32 2.4 15.7 1.0
O A:HOH133 2.5 20.8 1.0
O A:GLY30 2.5 11.8 1.0
O A:HOH126 2.5 11.5 1.0
CG A:ASP49 2.7 5.0 1.0
C A:TYR28 3.4 7.3 1.0
C A:GLY32 3.6 15.2 1.0
N A:GLY30 3.7 7.6 1.0
C A:GLY30 3.8 10.9 1.0
N A:GLY32 4.1 13.4 1.0
CA A:TYR28 4.1 6.0 1.0
CB A:ASP49 4.2 6.3 1.0
CA A:GLY32 4.3 14.5 1.0
C A:LEU31 4.4 12.4 1.0
N A:CYS29 4.4 6.5 1.0
O A:HOH127 4.4 11.9 1.0
C A:CYS29 4.4 7.2 1.0
CA A:GLY30 4.5 9.5 1.0
CA A:CYS29 4.5 7.2 1.0
O A:HOH128 4.5 7.6 1.0
N A:GLY33 4.6 14.4 1.0
O A:LEU31 4.7 13.5 1.0
CA A:GLY33 4.7 14.3 1.0
CB A:TYR28 4.7 4.8 1.0
N A:LEU31 4.7 12.2 1.0
O A:HOH181 4.8 47.0 1.0
CA A:LEU31 4.9 12.3 1.0

Reference:

B.W.Dijkstra, K.H.Kalk, J.Drenth, G.H.De Haas, M.R.Egmond, A.J.Slotboom. Role of the N-Terminus in the Interaction of Pancreatic Phospholipase A2 with Aggregated Substrates. Properties and Crystal Structure of Transaminated Phospholipase A2 Biochemistry V. 23 2759 1984.
ISSN: ISSN 0006-2960
PubMed: 6466614
DOI: 10.1021/BI00307A035
Page generated: Sat Jul 13 08:21:24 2024

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