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Calcium in PDB 5mnz: Neutron Structure of Cationic Trypsin in Its Apo Form

Enzymatic activity of Neutron Structure of Cationic Trypsin in Its Apo Form

All present enzymatic activity of Neutron Structure of Cationic Trypsin in Its Apo Form:
3.4.21.4;

Calcium Binding Sites:

The binding sites of Calcium atom in the Neutron Structure of Cationic Trypsin in Its Apo Form (pdb code 5mnz). 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 Neutron Structure of Cationic Trypsin in Its Apo Form, PDB code: 5mnz:

Calcium binding site 1 out of 1 in 5mnz

Go back to Calcium Binding Sites List in 5mnz
Calcium binding site 1 out of 1 in the Neutron Structure of Cationic Trypsin in Its Apo Form


Mono view


Stereo pair view

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

b:8.9
occ:1.00
O A:VAL75 2.2 9.3 1.0
OE1 A:GLU70 2.3 8.8 1.0
OE2 A:GLU80 2.3 10.1 1.0
O A:DOD464 2.3 11.9 1.0
O A:ASN72 2.3 9.0 1.0
O A:DOD414 2.4 12.4 1.0
D2 A:DOD464 2.8 11.5 1.0
D1 A:DOD414 2.9 13.6 1.0
D2 A:DOD414 2.9 12.8 1.0
D1 A:DOD464 3.2 15.8 1.0
HA A:VAL76 3.2 14.1 1.0
HG2 A:GLU80 3.3 12.4 1.0
D A:GLU77 3.3 12.8 1.0
H A:GLU77 3.3 12.8 0.0
CD A:GLU80 3.4 12.3 1.0
C A:VAL75 3.4 12.5 1.0
CD A:GLU70 3.4 7.1 1.0
H A:VAL75 3.4 13.8 0.1
D A:VAL75 3.4 13.8 0.9
HG3 A:GLU77 3.5 14.8 1.0
C A:ASN72 3.5 9.4 1.0
HA A:ILE73 3.6 12.1 1.0
CG A:GLU80 3.7 10.7 1.0
HG3 A:GLU80 3.7 12.4 1.0
D A:ASP71 3.7 10.5 0.9
H A:ASP71 3.7 10.5 0.1
OE2 A:GLU70 3.8 11.0 1.0
HA A:GLU70 3.8 11.4 1.0
CA A:VAL76 4.1 13.0 1.0
N A:GLU77 4.1 12.7 1.0
HB3 A:ASN72 4.1 12.8 1.0
HB2 A:GLU77 4.1 13.9 1.0
N A:VAL76 4.1 11.9 1.0
D A:ASN72 4.2 10.4 1.0
H A:ASN72 4.2 10.4 0.0
N A:VAL75 4.2 9.1 1.0
OE1 A:GLU77 4.3 13.7 1.0
CA A:ILE73 4.3 7.8 1.0
N A:ILE73 4.4 7.6 1.0
CG A:GLU77 4.4 13.4 1.0
N A:ASN72 4.4 7.7 1.0
CA A:VAL75 4.4 10.4 1.0
CA A:ASN72 4.5 9.5 1.0
OE1 A:GLU80 4.5 12.6 1.0
HB A:VAL75 4.6 14.5 1.0
C A:VAL76 4.6 12.1 1.0
HB3 A:GLU70 4.6 8.7 1.0
C A:ILE73 4.6 9.8 1.0
N A:ASP71 4.6 8.6 1.0
O A:DOD460 4.6 16.8 1.0
CG A:GLU70 4.7 8.1 1.0
CB A:GLU77 4.7 11.3 1.0
HG23 A:VAL76 4.7 16.8 1.0
D1 A:DOD430 4.7 11.5 1.0
D2 A:DOD460 4.7 18.7 1.0
CA A:GLU70 4.8 7.0 1.0
CD A:GLU77 4.8 16.0 1.0
CB A:ASN72 4.8 8.9 1.0
N A:ASN74 4.9 9.1 1.0
CB A:GLU70 4.9 8.7 1.0
HZ A:PHE82 4.9 17.1 1.0
O A:DOD534 4.9 18.5 1.0
D A:ASN74 4.9 9.8 1.0
H A:ASN74 4.9 9.8 0.0

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 08:32:06 2024

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