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Calcium in PDB 3veq: A Binary Complex Betwwen Bovine Pancreatic Trypsin and A Engineered Mutant Trypsin Inhibitor

Enzymatic activity of A Binary Complex Betwwen Bovine Pancreatic Trypsin and A Engineered Mutant Trypsin Inhibitor

All present enzymatic activity of A Binary Complex Betwwen Bovine Pancreatic Trypsin and A Engineered Mutant Trypsin Inhibitor:
3.4.21.4;

Protein crystallography data

The structure of A Binary Complex Betwwen Bovine Pancreatic Trypsin and A Engineered Mutant Trypsin Inhibitor, PDB code: 3veq was solved by U.Sen, S.Majumder, S.Khamrui, J.Dasgupta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.91 / 2.25
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 122.997, 39.826, 76.783, 90.00, 119.65, 90.00
R / Rfree (%) 21.8 / 27.4

Calcium Binding Sites:

The binding sites of Calcium atom in the A Binary Complex Betwwen Bovine Pancreatic Trypsin and A Engineered Mutant Trypsin Inhibitor (pdb code 3veq). 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 A Binary Complex Betwwen Bovine Pancreatic Trypsin and A Engineered Mutant Trypsin Inhibitor, PDB code: 3veq:

Calcium binding site 1 out of 1 in 3veq

Go back to Calcium Binding Sites List in 3veq
Calcium binding site 1 out of 1 in the A Binary Complex Betwwen Bovine Pancreatic Trypsin and A Engineered Mutant Trypsin Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of A Binary Complex Betwwen Bovine Pancreatic Trypsin and A Engineered Mutant Trypsin Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca301

b:30.1
occ:1.00
 OE2 B:GLU77 2.2 32.8 1.0
O B:VAL72 2.3 26.6 1.0
OE1 B:GLU67 2.3 21.9 1.0
O B:ASN69 2.4 26.7 1.0
CD B:GLU77 3.3 31.8 1.0
C B:VAL72 3.4 28.6 1.0
CD B:GLU67 3.4 22.6 1.0
C B:ASN69 3.6 27.5 1.0
CG B:GLU77 3.6 32.3 1.0
OE2 B:GLU67 3.7 23.1 1.0
CA B:VAL73 3.9 28.1 1.0
N B:VAL73 4.0 28.7 1.0
N B:GLU74 4.2 25.7 1.0
OE1 B:GLU74 4.2 32.5 1.0
CA B:ILE70 4.2 32.1 1.0
N B:VAL72 4.3 33.5 1.0
N B:ILE70 4.4 29.4 1.0
CG B:GLU74 4.4 27.1 1.0
OE1 B:GLU77 4.4 31.7 1.0
N B:ASN69 4.4 28.3 1.0
C B:VAL73 4.4 28.0 1.0
CA B:VAL72 4.4 31.1 1.0
C B:ILE70 4.5 33.0 1.0
CA B:ASN69 4.5 28.6 1.0
N B:ASP68 4.6 25.5 1.0
CD B:GLU74 4.7 29.0 1.0
O B:HOH431 4.7 31.5 1.0
CG B:GLU67 4.7 23.3 1.0
CB B:ASN69 4.7 27.3 1.0
O B:ILE70 4.8 35.1 1.0
CA B:GLU67 4.8 25.1 1.0
CB B:GLU74 4.8 26.6 1.0
CB B:GLU67 5.0 23.1 1.0
N B:ASN71 5.0 34.9 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: Tue Jul 8 17:34:05 2025

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