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Calcium in PDB 1esa: Direct Structure Observation of An Acyl-Enzyme Intermediate in the Hydrolysis of An Ester Substrate By Elastase

Enzymatic activity of Direct Structure Observation of An Acyl-Enzyme Intermediate in the Hydrolysis of An Ester Substrate By Elastase

All present enzymatic activity of Direct Structure Observation of An Acyl-Enzyme Intermediate in the Hydrolysis of An Ester Substrate By Elastase:
3.4.21.36;

Protein crystallography data

The structure of Direct Structure Observation of An Acyl-Enzyme Intermediate in the Hydrolysis of An Ester Substrate By Elastase, PDB code: 1esa was solved by X.Ding, B.Rasmussen, G.A.Petsko, D.Ringe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.370, 58.210, 74.830, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Direct Structure Observation of An Acyl-Enzyme Intermediate in the Hydrolysis of An Ester Substrate By Elastase (pdb code 1esa). 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 Direct Structure Observation of An Acyl-Enzyme Intermediate in the Hydrolysis of An Ester Substrate By Elastase, PDB code: 1esa:

Calcium binding site 1 out of 1 in 1esa

Go back to Calcium Binding Sites List in 1esa
Calcium binding site 1 out of 1 in the Direct Structure Observation of An Acyl-Enzyme Intermediate in the Hydrolysis of An Ester Substrate By Elastase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Direct Structure Observation of An Acyl-Enzyme Intermediate in the Hydrolysis of An Ester Substrate By Elastase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca280

b:23.1
occ:1.00
 O A:GLN79 2.4 20.7 1.0
O A:ASN76 2.5 12.4 1.0
OE2 A:GLU84 2.5 11.2 1.0
OE1 A:GLU74 2.6 15.8 1.0
OD1 A:ASN81 2.7 16.9 1.0
OE2 A:GLU74 3.3 14.3 1.0
CD A:GLU74 3.3 14.3 1.0
CD A:GLU84 3.5 12.2 1.0
C A:GLN79 3.5 21.4 1.0
C A:ASN76 3.6 11.1 1.0
CG A:ASN81 3.7 15.0 1.0
N A:ASN81 3.9 16.2 1.0
CG A:GLU84 4.0 10.2 1.0
N A:GLN79 4.1 21.7 1.0
N A:ASN76 4.2 9.7 1.0
CA A:ASN80 4.2 18.4 1.0
O A:HOH321 4.3 41.6 1.0
N A:ASN80 4.3 18.7 1.0
CA A:ASN76 4.3 10.9 1.0
CB A:ASN81 4.4 14.3 1.0
CA A:GLN79 4.5 22.1 1.0
C A:LEU77 4.5 15.3 1.0
N A:LEU77 4.5 11.5 1.0
C A:ASN80 4.5 18.3 1.0
OE1 A:GLU84 4.5 12.1 1.0
O A:LEU77 4.5 16.6 1.0
ND2 A:ASN81 4.5 13.1 1.0
CA A:LEU77 4.6 12.5 1.0
CB A:ASN76 4.6 10.6 1.0
CA A:ASN81 4.7 16.5 1.0
N A:HIS75 4.7 8.6 1.0
CG A:GLU74 4.8 11.0 1.0
OH A:TYR86 4.8 21.4 1.0
N A:ASN78 4.9 17.9 1.0

Reference:

X.Ding, B.F.Rasmussen, G.A.Petsko, D.Ringe. Direct Structural Observation of An Acyl-Enzyme Intermediate in the Hydrolysis of An Ester Substrate By Elastase. Biochemistry V. 33 9285 1994.
ISSN: ISSN 0006-2960
PubMed: 8049229
DOI: 10.1021/BI00197A032
Page generated: Thu Jul 11 07:56:08 2024

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