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Calcium in PDB 1y34: Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A Mutant

Enzymatic activity of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A Mutant

All present enzymatic activity of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A Mutant:
3.4.21.62;

Protein crystallography data

The structure of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A Mutant, PDB code: 1y34 was solved by E.S.Radisky, C.J.Lu, G.Kwan, D.E.Koshland Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 81.65 / 1.55
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.820, 93.820, 185.332, 90.00, 90.00, 120.00
R / Rfree (%) 15.5 / 18

Other elements in 1y34:

The structure of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A Mutant also contains other interesting chemical elements:

Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A Mutant (pdb code 1y34). 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 the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A Mutant, PDB code: 1y34:

Calcium binding site 1 out of 1 in 1y34

Go back to Calcium Binding Sites List in 1y34
Calcium binding site 1 out of 1 in the Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A Mutant


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 the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca1001

b:15.9
occ:1.00
 O E:LEU75 2.3 9.6 1.0
OD1 E:ASN77 2.3 9.4 1.0
OE1 E:GLN2 2.4 10.1 1.0
O E:ILE79 2.4 11.1 1.0
OD1 E:ASP41 2.5 10.7 1.0
O E:VAL81 2.5 11.9 1.0
CG E:ASP41 3.3 11.7 1.0
CG E:ASN77 3.3 10.6 1.0
OD2 E:ASP41 3.4 11.7 1.0
CD E:GLN2 3.4 10.3 1.0
C E:LEU75 3.5 9.6 1.0
C E:VAL81 3.5 9.6 1.0
C E:ILE79 3.6 11.2 1.0
CG E:GLN2 3.8 11.3 1.0
ND2 E:ASN77 3.8 12.1 1.0
N E:ASN77 3.9 10.5 1.0
N E:VAL81 4.1 10.3 1.0
N E:ILE79 4.2 10.9 1.0
N E:LEU82 4.3 10.7 1.0
CG1 E:ILE79 4.3 12.7 1.0
C E:GLY80 4.4 10.4 1.0
N E:LEU75 4.4 9.2 1.0
N E:ASN76 4.4 9.8 1.0
CA E:LEU75 4.4 9.6 1.0
CA E:LEU82 4.4 10.2 1.0
CA E:ILE79 4.4 12.3 1.0
CA E:VAL81 4.4 9.5 1.0
CB E:GLN2 4.5 9.2 1.0
O E:ASN77 4.5 10.7 1.0
CA E:ASN76 4.5 10.2 1.0
CB E:ASN77 4.5 10.5 1.0
C E:ASN77 4.5 10.7 1.0
CA E:ASN77 4.5 10.2 1.0
N E:GLY80 4.6 10.7 1.0
C E:ASN76 4.6 10.7 1.0
NE2 E:GLN2 4.6 10.6 1.0
CB E:LEU75 4.7 9.5 1.0
CB E:ASP41 4.7 10.3 1.0
CA E:GLY80 4.7 10.3 1.0
O E:GLY80 4.8 11.8 1.0
C E:ALA74 4.9 9.3 1.0

Reference:

E.S.Radisky, C.J.Lu, G.Kwan, D.E.Koshland Jr.. Role of the Intramolecular Hydrogen Bond Network in the Inhibitory Power of Chymotrypsin Inhibitor 2 Biochemistry V. 44 6823 2005.
ISSN: ISSN 0006-2960
PubMed: 15865427
DOI: 10.1021/BI047301W
Page generated: Fri Jul 12 07:57:35 2024

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