Atomistry » Calcium » PDB 1edm-1evu » 1elg
Atomistry »
  Calcium »
    PDB 1edm-1evu »
      1elg »

Calcium in PDB 1elg: Nature of the Inactivation of Elastase By N-Peptidyl-O- Aroyl Hydroxylamine As A Function of pH

Enzymatic activity of Nature of the Inactivation of Elastase By N-Peptidyl-O- Aroyl Hydroxylamine As A Function of pH

All present enzymatic activity of Nature of the Inactivation of Elastase By N-Peptidyl-O- Aroyl Hydroxylamine As A Function of pH:
3.4.21.36;

Protein crystallography data

The structure of Nature of the Inactivation of Elastase By N-Peptidyl-O- Aroyl Hydroxylamine As A Function of pH, PDB code: 1elg was solved by X.Ding, B.Rasmussen, H.-U.Demuth, D.Ringe, A.C.U.Steinmetz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.080, 58.040, 75.180, 90.00, 90.00, 90.00
R / Rfree (%) 17 / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Nature of the Inactivation of Elastase By N-Peptidyl-O- Aroyl Hydroxylamine As A Function of pH (pdb code 1elg). 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 Nature of the Inactivation of Elastase By N-Peptidyl-O- Aroyl Hydroxylamine As A Function of pH, PDB code: 1elg:

Calcium binding site 1 out of 1 in 1elg

Go back to Calcium Binding Sites List in 1elg
Calcium binding site 1 out of 1 in the Nature of the Inactivation of Elastase By N-Peptidyl-O- Aroyl Hydroxylamine As A Function of pH


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Nature of the Inactivation of Elastase By N-Peptidyl-O- Aroyl Hydroxylamine As A Function of pH within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca280

b:15.1
occ:1.00
 O A:GLN79 2.4 15.2 1.0
O A:HOH327 2.5 18.7 1.0
O A:ASN76 2.5 9.4 1.0
OE2 A:GLU84 2.5 9.4 1.0
OE1 A:GLU74 2.5 13.5 1.0
OD1 A:ASN81 2.6 12.5 1.0
OE2 A:GLU74 3.2 16.3 1.0
CD A:GLU74 3.2 14.1 1.0
CG A:ASN81 3.5 10.6 1.0
CD A:GLU84 3.5 9.8 1.0
C A:GLN79 3.5 18.7 1.0
C A:ASN76 3.6 8.4 1.0
N A:ASN81 3.9 13.9 1.0
CG A:GLU84 3.9 7.9 1.0
CB A:ASN81 4.1 10.4 1.0
N A:ASN76 4.1 7.2 1.0
N A:GLN79 4.2 19.0 1.0
CA A:ASN80 4.3 17.5 1.0
CA A:ASN76 4.3 7.8 1.0
N A:ASN80 4.3 17.3 1.0
ND2 A:ASN81 4.4 10.0 1.0
C A:ASN80 4.4 16.8 1.0
CA A:GLN79 4.5 19.6 1.0
N A:LEU77 4.5 8.1 1.0
OE1 A:GLU84 4.5 10.1 1.0
C A:LEU77 4.6 13.6 1.0
CB A:ASN76 4.6 9.0 1.0
CA A:LEU77 4.6 12.0 1.0
CA A:ASN81 4.6 13.1 1.0
O A:LEU77 4.6 13.5 1.0
CG A:GLU74 4.7 9.8 1.0
N A:HIS75 4.7 7.3 1.0
N A:ASN78 4.9 15.4 1.0

Reference:

X.Ding, B.F.Rasmussen, H.U.Demuth, D.Ringe, A.C.Steinmetz. Nature of the Inactivation of Elastase By N-Peptidyl-O-Aroyl Hydroxylamine As A Function of pH. Biochemistry V. 34 7749 1995.
ISSN: ISSN 0006-2960
PubMed: 7779821
DOI: 10.1021/BI00023A022
Page generated: Thu Jul 11 07:53:27 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy