Calcium in PDB 5mng: Cationic Trypsin in Complex with Benzamidine (Deuterated Sample at 100 K)

Enzymatic activity of Cationic Trypsin in Complex with Benzamidine (Deuterated Sample at 100 K)

All present enzymatic activity of Cationic Trypsin in Complex with Benzamidine (Deuterated Sample at 100 K):
3.4.21.4;

Protein crystallography data

The structure of Cationic Trypsin in Complex with Benzamidine (Deuterated Sample at 100 K), PDB code: 5mng 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) 24.67 / 0.86
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.486, 58.177, 66.833, 90.00, 90.00, 90.00
R / Rfree (%) 9.9 / 10.9

Calcium Binding Sites:

The binding sites of Calcium atom in the Cationic Trypsin in Complex with Benzamidine (Deuterated Sample at 100 K) (pdb code 5mng). 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 Complex with Benzamidine (Deuterated Sample at 100 K), PDB code: 5mng:

Calcium binding site 1 out of 1 in 5mng

Go back to Calcium Binding Sites List in 5mng
Calcium binding site 1 out of 1 in the Cationic Trypsin in Complex with Benzamidine (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 Complex with Benzamidine (Deuterated Sample at 100 K) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:5.8
occ:1.00
OE1 A:GLU70 2.3 6.6 1.0
O A:VAL75 2.3 6.6 1.0
O A:ASN72 2.3 6.2 1.0
OE2 A:GLU80 2.3 6.5 1.0
O A:HOH518 2.3 7.1 1.0
O A:HOH415 2.4 6.6 1.0
H1 A:HOH415 2.6 7.9 1.0
H1 A:HOH518 2.8 8.5 1.0
H2 A:HOH518 3.0 8.5 1.0
CD A:GLU70 3.3 5.9 1.0
HA A:VAL76 3.4 8.7 1.0
CD A:GLU80 3.4 6.5 1.0
HG2 A:GLU80 3.4 9.7 1.0
C A:VAL75 3.4 6.5 1.0
C A:ASN72 3.5 5.9 1.0
H A:GLU77 3.5 8.8 0.3
H A:GLU77 3.5 8.8 0.7
H A:VAL75 3.6 7.7 1.0
HA A:ILE73 3.6 7.0 1.0
HG3 A:GLU77 3.7 10.5 0.3
HG3 A:GLU80 3.7 9.7 1.0
HG3 A:GLU77 3.7 9.5 0.7
CG A:GLU80 3.8 8.1 1.0
OE2 A:GLU70 3.8 6.6 1.0
H A:ASP71 3.8 7.2 1.0
HA A:GLU70 3.9 6.8 1.0
CA A:VAL76 4.1 7.2 1.0
N A:GLU77 4.2 7.3 0.7
N A:GLU77 4.2 7.3 0.3
N A:VAL76 4.2 7.0 1.0
HB3 A:ASN72 4.2 8.5 1.0
N A:VAL75 4.2 6.4 1.0
OE1 A:GLU77 4.3 6.9 0.7
CA A:ILE73 4.3 5.8 1.0
H A:ASN72 4.3 7.3 1.0
N A:ILE73 4.3 5.9 1.0
OE1 A:GLU77 4.3 10.1 0.3
N A:ASN72 4.4 6.1 1.0
CA A:VAL75 4.4 6.6 1.0
CA A:ASN72 4.5 6.1 1.0
O A:HOH521 4.5 7.3 1.0
CG A:GLU77 4.5 7.9 0.7
CG A:GLU77 4.5 8.7 0.3
HB3 A:GLU70 4.5 6.8 1.0
H2 A:HOH521 4.5 8.8 1.0
OE1 A:GLU80 4.5 7.0 1.0
C A:ILE73 4.5 5.8 1.0
N A:ASP71 4.6 6.0 1.0
CG A:GLU70 4.6 6.0 1.0
HB A:VAL75 4.6 8.6 1.0
C A:VAL76 4.7 7.7 1.0
H2 A:HOH486 4.7 7.8 1.0
CA A:GLU70 4.7 5.7 1.0
CB A:GLU77 4.8 8.2 0.7
CD A:GLU77 4.8 7.8 0.7
HG22 A:VAL76 4.8 10.5 1.0
O A:HOH660 4.8 12.6 1.0
CB A:GLU77 4.8 8.0 0.3
CB A:GLU70 4.8 5.7 1.0
CB A:ASN72 4.8 7.1 1.0
N A:ASN74 4.9 5.8 1.0
CD A:GLU77 4.9 9.9 0.3
H A:ASN74 4.9 6.9 1.0
O A:ILE73 4.9 6.5 1.0
C A:ASP71 5.0 5.8 1.0
HG2 A:GLU70 5.0 7.2 1.0
H A:VAL76 5.0 8.4 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: Sat Dec 12 05:38:16 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy