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Calcium in PDB 8izh: Crystal Structure of Trypsin-Aminoguanidine Complex at 2.30 Angstroms Resolution

Enzymatic activity of Crystal Structure of Trypsin-Aminoguanidine Complex at 2.30 Angstroms Resolution

All present enzymatic activity of Crystal Structure of Trypsin-Aminoguanidine Complex at 2.30 Angstroms Resolution:
3.4.21.4;

Protein crystallography data

The structure of Crystal Structure of Trypsin-Aminoguanidine Complex at 2.30 Angstroms Resolution, PDB code: 8izh was solved by M.S.Ahmad, N.Kalam, Z.Akbar, S.Rasheed, M.I.Choudhary, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.64 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.59, 58.248, 66.326, 90, 90, 90
R / Rfree (%) 21.2 / 29.5

Other elements in 8izh:

The structure of Crystal Structure of Trypsin-Aminoguanidine Complex at 2.30 Angstroms Resolution also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Trypsin-Aminoguanidine Complex at 2.30 Angstroms Resolution (pdb code 8izh). 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 Crystal Structure of Trypsin-Aminoguanidine Complex at 2.30 Angstroms Resolution, PDB code: 8izh:

Calcium binding site 1 out of 1 in 8izh

Go back to Calcium Binding Sites List in 8izh
Calcium binding site 1 out of 1 in the Crystal Structure of Trypsin-Aminoguanidine Complex at 2.30 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Trypsin-Aminoguanidine Complex at 2.30 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:6.4
occ:1.00
 OE1 A:GLU70 2.2 4.7 1.0
O A:ASN72 2.2 4.3 1.0
O A:HOH464 2.2 8.3 1.0
O A:VAL75 2.3 5.0 1.0
O A:HOH409 2.3 5.6 1.0
OE2 A:GLU80 2.5 6.6 1.0
CD A:GLU70 3.3 4.7 1.0
C A:ASN72 3.4 4.3 1.0
C A:VAL75 3.4 5.0 1.0
CD A:GLU80 3.5 6.5 1.0
CG A:GLU80 3.8 6.6 1.0
OE2 A:GLU70 3.8 4.6 1.0
N A:VAL76 4.2 5.2 1.0
N A:ILE73 4.2 4.3 1.0
N A:GLU77 4.2 5.8 1.0
CA A:ILE73 4.2 4.4 1.0
CA A:VAL76 4.2 5.5 1.0
O A:HOH436 4.3 3.3 1.0
N A:VAL75 4.3 4.7 1.0
OE1 A:GLU77 4.3 5.9 1.0
N A:ASN72 4.3 4.3 1.0
CA A:ASN72 4.3 4.3 1.0
CA A:VAL75 4.4 4.8 1.0
CG A:GLU70 4.5 4.8 1.0
C A:ILE73 4.6 4.4 1.0
CG A:GLU77 4.6 6.0 1.0
N A:ASP71 4.6 4.5 1.0
OE1 A:GLU80 4.6 6.4 1.0
CA A:GLU70 4.7 4.8 1.0
C A:VAL76 4.7 5.7 1.0
CB A:GLU70 4.8 4.8 1.0
CB A:GLU77 4.8 6.0 1.0
CB A:ASN72 4.8 4.3 1.0
CD A:GLU77 4.8 6.0 1.0
N A:ASN74 4.9 4.4 1.0
C A:ASP71 4.9 4.4 1.0

Reference:

M.S.Ahmad, N.Kalam, Z.Akbar, N.Shah, S.Rasheed, M.I.Choudhary. Structural Basis For the Binding of Famotidine, Cimetidine, Guanidine, and Pimagedine with Serine Protease. Biochem.Biophys.Res.Commun. V. 733 50603 2024.
ISSN: ESSN 1090-2104
PubMed: 39216203
DOI: 10.1016/J.BBRC.2024.150603
Page generated: Thu Jul 10 05:26:02 2025

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