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Calcium in PDB 2o9q: The Crystal Structure of Bovine Trypsin Complexed with A Small Inhibition Peptide ORB2K

Enzymatic activity of The Crystal Structure of Bovine Trypsin Complexed with A Small Inhibition Peptide ORB2K

All present enzymatic activity of The Crystal Structure of Bovine Trypsin Complexed with A Small Inhibition Peptide ORB2K:
3.4.21.4;

Protein crystallography data

The structure of The Crystal Structure of Bovine Trypsin Complexed with A Small Inhibition Peptide ORB2K, PDB code: 2o9q was solved by J.Li, C.Zhang, X.Xu, J.Wang, W.Gong, R.Lai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 16.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.016, 63.451, 69.684, 90.00, 90.00, 90.00
R / Rfree (%) 15.5 / 19.5

Calcium Binding Sites:

The binding sites of Calcium atom in the The Crystal Structure of Bovine Trypsin Complexed with A Small Inhibition Peptide ORB2K (pdb code 2o9q). 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 The Crystal Structure of Bovine Trypsin Complexed with A Small Inhibition Peptide ORB2K, PDB code: 2o9q:

Calcium binding site 1 out of 1 in 2o9q

Go back to Calcium Binding Sites List in 2o9q
Calcium binding site 1 out of 1 in the The Crystal Structure of Bovine Trypsin Complexed with A Small Inhibition Peptide ORB2K


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Crystal Structure of Bovine Trypsin Complexed with A Small Inhibition Peptide ORB2K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca501

b:14.4
occ:1.00
OE2 A:GLU80 2.3 14.8 1.0
O A:VAL75 2.3 14.8 1.0
OE1 A:GLU70 2.4 13.8 1.0
O A:ASN72 2.4 14.0 1.0
O4 A:SO41001 2.4 8.1 0.6
O A:HOH1080 2.4 16.2 1.0
O1 A:SO41001 2.6 11.2 0.6
S A:SO41001 3.1 13.8 0.6
CD A:GLU80 3.3 15.7 1.0
CD A:GLU70 3.5 14.9 1.0
C A:VAL75 3.5 15.8 1.0
C A:ASN72 3.6 13.8 1.0
CG A:GLU80 3.6 15.3 1.0
OE2 A:GLU70 3.9 14.5 1.0
O3 A:SO41001 4.1 11.3 0.6
O2 A:SO41001 4.1 13.8 0.6
CA A:VAL76 4.2 16.2 1.0
N A:VAL76 4.3 15.0 1.0
N A:GLU77 4.4 17.3 1.0
CA A:ILE73 4.4 13.3 1.0
OE1 A:GLU80 4.4 13.7 1.0
N A:ILE73 4.4 12.9 1.0
N A:VAL75 4.4 14.8 1.0
N A:ASN72 4.5 13.9 1.0
CA A:ASN72 4.5 13.8 1.0
CA A:VAL75 4.5 14.9 1.0
O A:HOH1150 4.6 37.7 1.0
C A:ILE73 4.7 13.5 1.0
CB A:ASN72 4.7 14.3 1.0
CG A:GLU70 4.7 14.7 1.0
N A:ASP71 4.7 13.5 1.0
C A:VAL76 4.8 17.0 1.0
O A:HOH1062 4.8 18.3 1.0
CA A:GLU70 4.9 13.9 1.0
O A:HOH1276 4.9 25.4 1.0
CB A:GLU70 4.9 14.7 1.0

Reference:

J.Li, C.Zhang, X.Xu, J.Wang, H.Yang, C.Xu, D.Ma, Y.Wang, W.Gong, R.Lai. From Protease Inhibitor to Antibiotics: Single Point Mutation Makes Tremendous Functional Shift To Be Published.
Page generated: Fri Jul 12 14:36:41 2024

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