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Calcium in PDB 1ceh: Structure and Function of the Catalytic Site Mutant ASP99ASN of Phospholipase A2: Absence of Conserved Structural Water

Enzymatic activity of Structure and Function of the Catalytic Site Mutant ASP99ASN of Phospholipase A2: Absence of Conserved Structural Water

All present enzymatic activity of Structure and Function of the Catalytic Site Mutant ASP99ASN of Phospholipase A2: Absence of Conserved Structural Water:
3.1.1.4;

Protein crystallography data

The structure of Structure and Function of the Catalytic Site Mutant ASP99ASN of Phospholipase A2: Absence of Conserved Structural Water, PDB code: 1ceh was solved by A.Kumar, C.Sekharudu, B.Ramakrishnan, C.M.Dupureur, H.Zhu, M.-D.Tsai, M.Sundaralingam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.50 / 1.90
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 46.110, 46.110, 102.100, 90.00, 90.00, 120.00
R / Rfree (%) 18.5 / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure and Function of the Catalytic Site Mutant ASP99ASN of Phospholipase A2: Absence of Conserved Structural Water (pdb code 1ceh). 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 Structure and Function of the Catalytic Site Mutant ASP99ASN of Phospholipase A2: Absence of Conserved Structural Water, PDB code: 1ceh:

Calcium binding site 1 out of 1 in 1ceh

Go back to Calcium Binding Sites List in 1ceh
Calcium binding site 1 out of 1 in the Structure and Function of the Catalytic Site Mutant ASP99ASN of Phospholipase A2: Absence of Conserved Structural Water


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure and Function of the Catalytic Site Mutant ASP99ASN of Phospholipase A2: Absence of Conserved Structural Water within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca124

b:12.1
occ:1.00
 O A:TYR28 1.9 15.3 1.0
O A:GLY32 2.0 22.4 1.0
O A:GLY30 2.1 20.3 1.0
O A:HOH238 2.3 52.5 1.0
OD2 A:ASP49 2.4 19.8 1.0
O A:HOH204 2.5 15.8 1.0
OD1 A:ASP49 2.6 16.4 1.0
CG A:ASP49 2.9 17.4 1.0
C A:TYR28 3.1 15.2 1.0
C A:GLY32 3.2 23.2 1.0
C A:GLY30 3.3 21.8 1.0
N A:GLY30 3.8 19.7 1.0
N A:GLY32 4.1 26.5 1.0
O A:HOH216 4.1 21.3 1.0
CA A:GLY32 4.1 24.0 1.0
CA A:TYR28 4.1 12.6 1.0
N A:CYS29 4.1 14.8 1.0
C A:LEU31 4.2 26.3 1.0
CA A:GLY30 4.2 20.2 1.0
N A:GLY33 4.2 26.1 1.0
N A:LEU31 4.3 26.4 1.0
CB A:ASP49 4.4 15.1 1.0
O A:HOH237 4.4 32.5 1.0
CA A:CYS29 4.4 16.4 1.0
O A:LEU31 4.5 26.9 1.0
C A:CYS29 4.5 16.3 1.0
CA A:LEU31 4.5 28.4 1.0
CA A:GLY33 4.6 26.4 1.0
CB A:TYR28 4.6 11.4 1.0
O A:HOH230 4.7 24.2 1.0
O A:CYS45 4.9 10.4 1.0

Reference:

A.Kumar, C.Sekharudu, B.Ramakrishnan, C.M.Dupureur, H.Zhu, M.D.Tsai, M.Sundaralingam. Structure and Function of the Catalytic Site Mutant Asp 99 Asn of Phospholipase A2: Absence of the Conserved Structural Water. Protein Sci. V. 3 2082 1994.
ISSN: ISSN 0961-8368
PubMed: 7703854
Page generated: Mon Jul 7 13:57:37 2025

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