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Calcium in PDB 3i29: Crystal Structure of A Binary Complex Between An Mutant Trypsin Inhibitor with Bovine Trypsin

Enzymatic activity of Crystal Structure of A Binary Complex Between An Mutant Trypsin Inhibitor with Bovine Trypsin

All present enzymatic activity of Crystal Structure of A Binary Complex Between An Mutant Trypsin Inhibitor with Bovine Trypsin:
3.4.21.4;

Protein crystallography data

The structure of Crystal Structure of A Binary Complex Between An Mutant Trypsin Inhibitor with Bovine Trypsin, PDB code: 3i29 was solved by S.Khamrui, S.Majumder, J.Dasgupta, J.K.Dattagupta, U.Sen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 9.99 / 2.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 123.098, 39.729, 76.601, 90.00, 120.00, 90.00
R / Rfree (%) 21.9 / 28.7

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of A Binary Complex Between An Mutant Trypsin Inhibitor with Bovine Trypsin (pdb code 3i29). 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 A Binary Complex Between An Mutant Trypsin Inhibitor with Bovine Trypsin, PDB code: 3i29:

Calcium binding site 1 out of 1 in 3i29

Go back to Calcium Binding Sites List in 3i29
Calcium binding site 1 out of 1 in the Crystal Structure of A Binary Complex Between An Mutant Trypsin Inhibitor with Bovine Trypsin


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 A Binary Complex Between An Mutant Trypsin Inhibitor with Bovine Trypsin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca991

b:38.4
occ:1.00
 O A:VAL75 2.0 22.0 1.0
OE2 A:GLU80 2.2 27.5 1.0
OE1 A:GLU70 2.3 25.0 1.0
O A:ASN72 2.3 27.1 1.0
C A:VAL75 3.1 22.6 1.0
CD A:GLU80 3.3 22.8 1.0
CD A:GLU70 3.5 22.3 1.0
C A:ASN72 3.5 24.1 1.0
CG A:GLU80 3.6 22.3 1.0
CA A:VAL76 3.7 20.2 1.0
N A:VAL76 3.8 21.9 1.0
N A:GLU77 3.8 20.7 1.0
OE1 A:GLU77 3.9 24.9 1.0
OE2 A:GLU70 4.0 25.1 1.0
CG A:GLU77 4.0 22.7 1.0
C A:VAL76 4.1 21.8 1.0
N A:VAL75 4.3 26.0 1.0
CA A:VAL75 4.3 24.4 1.0
O A:HOH306 4.3 22.6 1.0
N A:ASN72 4.3 24.0 1.0
OE1 A:GLU80 4.4 19.7 1.0
CA A:ASN72 4.4 24.8 1.0
CD A:GLU77 4.4 24.8 1.0
N A:ILE73 4.4 25.2 1.0
CB A:ASN72 4.5 22.1 1.0
CA A:ILE73 4.5 26.1 1.0
CB A:GLU77 4.5 21.5 1.0
C A:ILE73 4.7 26.1 1.0
CG A:GLU70 4.7 23.0 1.0
N A:ASP71 4.8 21.2 1.0
CA A:GLU77 4.8 21.3 1.0
CG1 A:VAL75 4.9 22.8 1.0
O A:ILE73 5.0 24.9 1.0

Reference:

S.Majumder, S.Khamrui, J.Dasgupta, J.K.Dattagupta, U.Sen. Role of Remote Scaffolding Residues in the Inhibitory Loop Pre-Organization, Flexibility, Rigidification and Enzyme Inhibition of Serine Protease Inhibitors Biochim.Biophys.Acta V.1824 882 2012.
ISSN: ISSN 0006-3002
PubMed: 22709512
DOI: 10.1016/J.BBAPAP.2012.04.009
Page generated: Sat Jul 13 11:21:14 2024

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