Atomistry » Calcium » PDB 5mi4-5moo » 5mnf
Atomistry »
  Calcium »
    PDB 5mi4-5moo »
      5mnf »

Calcium in PDB 5mnf: Cationic Trypsin in Its Apo Form (Deuterated Sample at 295 K)

Enzymatic activity of Cationic Trypsin in Its Apo Form (Deuterated Sample at 295 K)

All present enzymatic activity of Cationic Trypsin in Its Apo Form (Deuterated Sample at 295 K):
3.4.21.4;

Protein crystallography data

The structure of Cationic Trypsin in Its Apo Form (Deuterated Sample at 295 K), PDB code: 5mnf 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) 19.23 / 0.99
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.999, 58.623, 67.565, 90.00, 90.00, 90.00
R / Rfree (%) 9.6 / 10.7

Calcium Binding Sites:

The binding sites of Calcium atom in the Cationic Trypsin in Its Apo Form (Deuterated Sample at 295 K) (pdb code 5mnf). 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 295 K), PDB code: 5mnf:

Calcium binding site 1 out of 1 in 5mnf

Go back to Calcium Binding Sites List in 5mnf
Calcium binding site 1 out of 1 in the Cationic Trypsin in Its Apo Form (Deuterated Sample at 295 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 295 K) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:8.4
occ:1.00
OE1 A:GLU70 2.3 10.0 1.0
O A:VAL75 2.3 9.8 1.0
OE2 A:GLU80 2.3 9.8 1.0
O A:ASN72 2.3 8.8 1.0
O A:HOH465 2.4 11.5 1.0
O A:HOH403 2.4 10.0 1.0
H1 A:HOH403 2.6 12.0 1.0
H2 A:HOH403 3.1 12.0 1.0
CD A:GLU70 3.4 8.6 1.0
HA A:VAL76 3.4 13.0 1.0
HG2 A:GLU80 3.4 14.8 1.0
CD A:GLU80 3.4 9.7 1.0
C A:VAL75 3.4 9.1 1.0
C A:ASN72 3.5 7.7 1.0
H A:GLU77 3.5 12.8 1.0
H A:VAL75 3.6 10.6 1.0
HG3 A:GLU77 3.7 14.5 1.0
CG A:GLU80 3.8 12.3 1.0
OE2 A:GLU70 3.8 10.7 1.0
H A:ASP71 3.8 9.9 1.0
HA A:GLU70 3.9 9.8 1.0
CA A:VAL76 4.1 10.8 1.0
N A:GLU77 4.2 10.6 1.0
HB3 A:ASN72 4.2 11.7 1.0
N A:VAL76 4.2 9.8 1.0
N A:VAL75 4.2 8.8 1.0
HB2 A:GLU77 4.3 14.2 1.0
OE1 A:GLU77 4.3 11.9 1.0
CA A:ILE73 4.3 8.3 1.0
N A:ILE73 4.3 7.9 1.0
N A:ASN72 4.4 8.3 1.0
CA A:VAL75 4.5 9.5 1.0
CA A:ASN72 4.5 8.3 1.0
HB3 A:GLU70 4.5 9.7 1.0
O A:HOH464 4.5 12.7 1.0
CG A:GLU77 4.5 12.1 1.0
OE1 A:GLU80 4.5 10.9 1.0
C A:ILE73 4.6 8.1 1.0
N A:ASP71 4.6 8.2 1.0
CG A:GLU70 4.6 8.5 1.0
HB A:VAL75 4.6 13.1 1.0
C A:VAL76 4.7 11.1 1.0
CA A:GLU70 4.7 8.1 1.0
CB A:GLU77 4.8 11.8 1.0
CB A:GLU70 4.8 8.1 1.0
CD A:GLU77 4.8 13.3 1.0
CB A:ASN72 4.8 9.7 1.0
O A:HOH563 4.9 25.9 1.0
N A:ASN74 4.9 8.1 1.0
H A:ASN74 4.9 9.7 1.0
O A:ILE73 5.0 9.7 1.0
HG2 A:GLU70 5.0 10.2 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: Mon Jul 15 08:29:56 2024

Last articles

Zn in 1MC5
Zn in 1MFM
Zn in 1MA0
Zn in 1MED
Zn in 1MEA
Zn in 1MBX
Zn in 1MA3
Zn in 1M9O
Zn in 1M9R
Zn in 1M9Q
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy