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Calcium in PDB 6t5w: Cationic Trypsin in Complex with A D-Phe-Pro-P-Aminopyridine Derivative (Cocrystallizaton at 291 K)

Enzymatic activity of Cationic Trypsin in Complex with A D-Phe-Pro-P-Aminopyridine Derivative (Cocrystallizaton at 291 K)

All present enzymatic activity of Cationic Trypsin in Complex with A D-Phe-Pro-P-Aminopyridine Derivative (Cocrystallizaton at 291 K):
3.4.21.4;

Protein crystallography data

The structure of Cationic Trypsin in Complex with A D-Phe-Pro-P-Aminopyridine Derivative (Cocrystallizaton at 291 K), PDB code: 6t5w was solved by K.Ngo, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.11 / 1.13
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.019, 56.845, 66.155, 90.00, 90.00, 90.00
R / Rfree (%) 12.8 / 14.5

Calcium Binding Sites:

The binding sites of Calcium atom in the Cationic Trypsin in Complex with A D-Phe-Pro-P-Aminopyridine Derivative (Cocrystallizaton at 291 K) (pdb code 6t5w). 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 A D-Phe-Pro-P-Aminopyridine Derivative (Cocrystallizaton at 291 K), PDB code: 6t5w:

Calcium binding site 1 out of 1 in 6t5w

Go back to Calcium Binding Sites List in 6t5w
Calcium binding site 1 out of 1 in the Cationic Trypsin in Complex with A D-Phe-Pro-P-Aminopyridine Derivative (Cocrystallizaton at 291 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 A D-Phe-Pro-P-Aminopyridine Derivative (Cocrystallizaton at 291 K) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:9.6
occ:1.00
 O A:VAL75 2.3 10.3 1.0
OE1 A:GLU70 2.3 10.3 1.0
O A:ASN72 2.3 10.5 1.0
OE2 A:GLU80 2.3 10.4 1.0
O A:HOH462 2.4 11.0 1.0
O A:HOH408 2.4 11.2 1.0
CD A:GLU70 3.3 9.4 1.0
HA A:VAL76 3.4 13.4 1.0
HG2 A:GLU80 3.4 14.5 1.0
CD A:GLU80 3.4 10.9 1.0
C A:VAL75 3.4 9.9 1.0
C A:ASN72 3.5 10.0 1.0
H A:GLU77 3.5 13.6 1.0
HA A:ILE73 3.5 12.5 1.0
H A:VAL75 3.6 11.8 1.0
HG3 A:GLU77 3.7 15.9 1.0
CG A:GLU80 3.7 12.1 1.0
HG3 A:GLU80 3.8 14.5 1.0
OE2 A:GLU70 3.8 10.4 1.0
H A:ASP71 3.8 12.4 1.0
HA A:GLU70 3.9 11.3 1.0
CA A:VAL76 4.1 11.2 1.0
N A:GLU77 4.2 11.3 1.0
N A:VAL76 4.2 10.3 1.0
HB3 A:ASN72 4.2 12.7 1.0
CA A:ILE73 4.2 10.4 1.0
N A:VAL75 4.2 9.8 1.0
HB2 A:GLU77 4.3 15.2 1.0
H A:ASN72 4.3 12.7 1.0
OE1 A:GLU77 4.3 12.6 1.0
N A:ILE73 4.3 9.9 1.0
N A:ASN72 4.4 10.5 1.0
CA A:ASN72 4.4 10.4 1.0
CA A:VAL75 4.4 10.4 1.0
CG A:GLU77 4.5 13.2 1.0
O A:HOH499 4.5 12.7 1.0
HB3 A:GLU70 4.5 11.4 1.0
C A:ILE73 4.5 9.0 1.0
OE1 A:GLU80 4.5 11.0 1.0
N A:ASP71 4.6 10.4 1.0
CG A:GLU70 4.6 10.1 1.0
C A:VAL76 4.6 11.2 1.0
HB A:VAL75 4.6 13.2 1.0
CA A:GLU70 4.7 9.4 1.0
CB A:GLU77 4.8 12.7 1.0
CD A:GLU77 4.8 14.2 1.0
CB A:GLU70 4.8 9.5 1.0
CB A:ASN72 4.8 10.6 1.0
HG22 A:VAL76 4.9 15.9 1.0
O A:ILE73 4.9 9.9 1.0
N A:ASN74 4.9 9.2 1.0
HZ A:PHE82 4.9 16.8 1.0
H A:ASN74 5.0 11.1 1.0
C A:ASP71 5.0 10.0 1.0
H A:VAL76 5.0 12.4 1.0
HG2 A:GLU70 5.0 12.1 1.0

Reference:

K.Ngo, C.Collins-Kautz, S.Gerstenecker, B.Wagner, A.Heine, G.Klebe. Protein-Induced Change in Ligand Protonation During Trypsin and Thrombin Binding: Hint on Differences in Selectivity Determinants of Both Proteins? J.Med.Chem. V. 63 3274 2020.
ISSN: ISSN 0022-2623
PubMed: 32011145
DOI: 10.1021/ACS.JMEDCHEM.9B02061
Page generated: Tue Jul 16 15:06:55 2024

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