Atomistry » Calcium » PDB 5mi5-5mop » 5mne
Atomistry »
  Calcium »
    PDB 5mi5-5mop »
      5mne »

Calcium in PDB 5mne: Cationic Trypsin in Its Apo Form (Deuterated Sample at 100 K)

Enzymatic activity of Cationic Trypsin in Its Apo Form (Deuterated Sample at 100 K)

All present enzymatic activity of Cationic Trypsin in Its Apo Form (Deuterated Sample at 100 K):
3.4.21.4;

Protein crystallography data

The structure of Cationic Trypsin in Its Apo Form (Deuterated Sample at 100 K), PDB code: 5mne was solved by J.Schiebel, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.75 / 1.01
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.669, 58.290, 66.861, 90.00, 90.00, 90.00
R / Rfree (%) 10.6 / 12.5

Calcium Binding Sites:

The binding sites of Calcium atom in the Cationic Trypsin in Its Apo Form (Deuterated Sample at 100 K) (pdb code 5mne). 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 Cationic Trypsin in Its Apo Form (Deuterated Sample at 100 K), PDB code: 5mne:

Calcium binding site 1 out of 1 in 5mne

Go back to Calcium Binding Sites List in 5mne
Calcium binding site 1 out of 1 in the Cationic Trypsin in Its Apo Form (Deuterated Sample at 100 K)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cationic Trypsin in Its Apo Form (Deuterated Sample at 100 K) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:7.6
occ:1.00
OE1 A:GLU70 2.3 8.4 1.0
O A:VAL75 2.3 8.5 1.0
OE2 A:GLU80 2.3 8.5 1.0
O A:ASN72 2.3 8.0 1.0
O A:HOH529 2.4 9.0 1.0
O A:HOH413 2.4 8.7 1.0
CD A:GLU70 3.3 7.6 1.0
HA A:VAL76 3.4 10.5 1.0
HG2 A:GLU80 3.4 12.3 1.0
CD A:GLU80 3.4 8.6 1.0
C A:VAL75 3.4 8.0 1.0
C A:ASN72 3.5 7.6 1.0
H A:GLU77 3.5 10.4 1.0
H A:VAL75 3.5 9.4 1.0
HA A:ILE73 3.6 9.3 1.0
HG3 A:GLU77 3.7 11.7 1.0
CG A:GLU80 3.8 10.2 1.0
OE2 A:GLU70 3.8 8.6 1.0
H A:ASP71 3.8 9.5 1.0
HA A:GLU70 3.9 9.3 1.0
CA A:VAL76 4.1 8.8 1.0
N A:GLU77 4.2 8.7 1.0
N A:VAL76 4.2 8.7 1.0
HB3 A:ASN72 4.2 10.9 1.0
N A:VAL75 4.2 7.8 1.0
OE1 A:GLU77 4.3 9.8 1.0
CA A:ILE73 4.3 7.7 1.0
H A:ASN72 4.3 9.5 1.0
N A:ILE73 4.3 7.7 1.0
N A:ASN72 4.4 7.9 1.0
CA A:VAL75 4.4 8.5 1.0
O A:HOH532 4.5 9.5 1.0
CA A:ASN72 4.5 7.9 1.0
HB3 A:GLU70 4.5 8.9 1.0
CG A:GLU77 4.5 9.8 1.0
OE1 A:GLU80 4.5 9.1 1.0
C A:ILE73 4.5 7.7 1.0
N A:ASP71 4.6 7.9 1.0
CG A:GLU70 4.6 7.8 1.0
HB A:VAL75 4.6 10.8 1.0
C A:VAL76 4.7 9.7 1.0
CA A:GLU70 4.7 7.7 1.0
CB A:GLU77 4.8 10.2 1.0
CD A:GLU77 4.8 11.4 1.0
CB A:GLU70 4.8 7.4 1.0
O A:HOH638 4.8 13.6 1.0
CB A:ASN72 4.8 9.1 1.0
N A:ASN74 4.9 7.5 1.0
HG22 A:VAL76 4.9 12.3 1.0
H A:ASN74 4.9 9.0 1.0
O A:ILE73 4.9 8.3 1.0
C A:ASP71 5.0 7.7 1.0
H A:VAL76 5.0 10.5 1.0
HG2 A:GLU70 5.0 9.3 1.0

Reference:

J.Schiebel, R.Gaspari, T.Wulsdorf, K.Ngo, C.Sohn, T.E.Schrader, A.Cavalli, A.Ostermann, A.Heine, G.Klebe. Intriguing Role of Water in Protein-Ligand Binding Studied By Neutron Crystallography on Trypsin Complexes. Nat Commun V. 9 3559 2018.
ISSN: ESSN 2041-1723
PubMed: 30177695
DOI: 10.1038/S41467-018-05769-2
Page generated: Wed Jul 9 08:27:18 2025

Last articles

Ca in 7JFR
Ca in 7JGI
Ca in 7G7Z
Ca in 7G7Y
Ca in 7GI3
Ca in 7G7X
Ca in 7G7V
Ca in 7G7W
Ca in 7G7U
Ca in 7G7T
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy