Atomistry » Calcium » PDB 1iqj-1j1n » 1irb
Atomistry »
  Calcium »
    PDB 1iqj-1j1n »
      1irb »

Calcium in PDB 1irb: Carboxylic Ester Hydrolase

Enzymatic activity of Carboxylic Ester Hydrolase

All present enzymatic activity of Carboxylic Ester Hydrolase:
3.1.1.4;

Protein crystallography data

The structure of Carboxylic Ester Hydrolase, PDB code: 1irb was solved by M.Sundaralingam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.90
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 46.810, 46.810, 102.890, 90.00, 90.00, 120.00
R / Rfree (%) 19.2 / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Carboxylic Ester Hydrolase (pdb code 1irb). 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 Carboxylic Ester Hydrolase, PDB code: 1irb:

Calcium binding site 1 out of 1 in 1irb

Go back to Calcium Binding Sites List in 1irb
Calcium binding site 1 out of 1 in the Carboxylic Ester Hydrolase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Carboxylic Ester Hydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca124

b:31.5
occ:1.00
O A:GLY30 1.9 23.4 1.0
O A:GLY32 2.0 29.1 1.0
O A:TYR28 2.1 17.2 1.0
O A:HOH204 2.6 44.0 1.0
OD2 A:ASP49 2.7 20.5 1.0
O A:HOH205 2.8 47.2 1.0
OD1 A:ASP49 3.0 20.7 1.0
C A:GLY30 3.1 19.4 1.0
CG A:ASP49 3.2 20.7 1.0
C A:GLY32 3.2 30.0 1.0
C A:TYR28 3.2 14.8 1.0
N A:GLY30 3.5 16.2 1.0
N A:GLY32 3.8 32.5 1.0
C A:LEU31 3.9 32.0 1.0
CA A:TYR28 4.0 14.8 1.0
CA A:GLY30 4.0 17.5 1.0
CA A:GLY32 4.0 30.7 1.0
N A:LEU31 4.1 26.0 1.0
N A:GLY33 4.2 30.9 1.0
O A:LEU31 4.3 36.7 1.0
N A:CYS29 4.3 14.6 1.0
CA A:LEU31 4.3 31.3 1.0
O A:HOH213 4.4 19.7 1.0
C A:CYS29 4.4 17.2 1.0
CA A:CYS29 4.5 14.8 1.0
CA A:GLY33 4.5 31.8 1.0
CB A:TYR28 4.6 10.8 1.0
CB A:ASP49 4.7 16.6 1.0
O A:HOH221 4.8 35.1 1.0
O A:CYS45 5.0 14.6 1.0

Reference:

B.Huang, B.Z.Yu, J.Rogers, I.J.Byeon, K.Sekar, X.Chen, M.Sundaralingam, M.D.Tsai, M.K.Jain. Phospholipase A2 Engineering. Deletion of the C-Terminus Segment Changes Substrate Specificity and Uncouples Calcium and Substrate Binding at the Zwitterionic Interface. Biochemistry V. 35 12164 1996.
ISSN: ISSN 0006-2960
PubMed: 8810924
DOI: 10.1021/BI960234O
Page generated: Thu Jul 11 10:26:01 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