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Calcium in PDB 3q3q: Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1

Enzymatic activity of Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1

All present enzymatic activity of Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1:
3.1.3.1;

Protein crystallography data

The structure of Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1, PDB code: 3q3q was solved by S.C.Bihani, M.V.Hosur, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.78 / 1.95
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 87.370, 87.370, 168.160, 90.00, 90.00, 90.00
R / Rfree (%) 15.5 / 18.6

Other elements in 3q3q:

The structure of Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1 also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1 (pdb code 3q3q). 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 Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1, PDB code: 3q3q:

Calcium binding site 1 out of 1 in 3q3q

Go back to Calcium Binding Sites List in 3q3q
Calcium binding site 1 out of 1 in the Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Spap: An Novel Alkaline Phosphatase From Bacterium Sphingomonas Sp. Strain Bsar-1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca566

b:35.2
occ:1.00
 O A:ASP553 2.4 37.0 1.0
O A:GLY551 2.4 39.4 1.0
OD2 A:ASP547 2.4 34.2 1.0
O A:VAL549 2.4 31.4 1.0
O A:HOH630 2.6 39.0 1.0
CG A:ASP547 3.3 33.0 1.0
C A:ASP553 3.5 46.9 1.0
C A:GLY551 3.5 34.8 1.0
C A:VAL549 3.6 26.8 1.0
OD1 A:ASP547 3.6 34.0 1.0
N A:GLY551 4.0 32.9 1.0
C A:ALA550 4.1 33.4 1.0
CA A:ASP554 4.1 46.2 1.0
C A:LYS552 4.1 42.4 1.0
O A:LYS552 4.2 39.4 1.0
N A:ASP554 4.2 44.7 1.0
N A:ASP553 4.2 39.2 1.0
O A:ALA550 4.3 32.8 1.0
CA A:GLY551 4.3 35.8 1.0
CB A:VAL549 4.4 39.4 1.0
CA A:VAL549 4.4 32.1 1.0
CA A:ASP553 4.5 42.7 1.0
N A:LYS552 4.5 38.9 1.0
CB A:ASP554 4.5 49.6 1.0
N A:ALA550 4.5 29.4 1.0
CA A:ALA550 4.6 35.4 1.0
CB A:ASP547 4.6 34.6 1.0
CA A:LYS552 4.7 43.1 1.0
CG1 A:VAL549 4.7 37.4 1.0
N A:VAL549 4.7 33.8 1.0
CG A:ASP554 5.0 59.3 1.0
O A:HOH755 5.0 49.9 1.0

Reference:

S.C.Bihani, A.Das, K.S.Nilgiriwala, V.Prashar, M.Pirocchi, S.K.Apte, J.-L.Ferrer, M.V.Hosur. X-Ray Structure Reveals A New Class and Provides Insight Into Evolution of Alkaline Phosphatases Plos One V. 6 22767 2011.
ISSN: ESSN 1932-6203
PubMed: 21829507
DOI: 10.1371/JOURNAL.PONE.0022767
Page generated: Sat Jul 13 17:14:42 2024

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