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Calcium in PDB 1lw6: Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 at 1.5 Angstrom Resolution

Enzymatic activity of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 at 1.5 Angstrom Resolution

All present enzymatic activity of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 at 1.5 Angstrom Resolution:
3.4.21.62;

Protein crystallography data

The structure of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 at 1.5 Angstrom Resolution, PDB code: 1lw6 was solved by E.S.Radisky, D.E.Koshland Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.66 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.332, 56.597, 118.635, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 18.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 at 1.5 Angstrom Resolution (pdb code 1lw6). 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 at 1.5 Angstrom Resolution, PDB code: 1lw6:

Calcium binding site 1 out of 1 in 1lw6

Go back to Calcium Binding Sites List in 1lw6
Calcium binding site 1 out of 1 in the Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 at 1.5 Angstrom 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 the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 at 1.5 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca300

b:7.5
occ:1.00
 O E:LEU75 2.5 7.6 1.0
OE1 E:GLN2 2.5 9.7 1.0
O E:VAL81 2.5 8.7 1.0
O E:ILE79 2.5 10.2 1.0
OD1 E:ASN77 2.5 10.3 1.0
OD2 E:ASP41 2.6 9.7 1.0
OD1 E:ASP41 2.6 9.1 1.0
CG E:ASP41 2.9 9.6 1.0
CG E:ASN77 3.5 10.1 1.0
CD E:GLN2 3.5 9.7 1.0
C E:LEU75 3.6 7.8 1.0
C E:VAL81 3.7 8.4 1.0
C E:ILE79 3.7 10.3 1.0
N E:VAL81 3.8 9.3 1.0
ND2 E:ASN77 3.8 10.6 1.0
CG E:GLN2 3.9 9.4 1.0
N E:ASN77 4.0 8.8 1.0
C E:GLY80 4.2 9.4 1.0
CA E:VAL81 4.3 8.4 1.0
CG1 E:ILE79 4.4 10.9 1.0
N E:LEU75 4.4 7.2 1.0
N E:ILE79 4.4 11.4 1.0
CB E:ASP41 4.4 8.9 1.0
CA E:LEU75 4.5 8.2 1.0
CA E:GLY80 4.5 9.5 1.0
N E:GLY80 4.5 9.7 1.0
CB E:GLN2 4.5 9.9 1.0
N E:ASN76 4.5 8.8 1.0
CA E:ILE79 4.6 11.1 1.0
NE2 E:GLN2 4.6 9.0 1.0
CA E:ASN76 4.6 8.5 1.0
N E:LEU82 4.6 8.2 1.0
CB E:ASN77 4.7 9.6 1.0
CA E:ASN77 4.7 9.5 1.0
C E:ASN77 4.7 10.7 1.0
O E:ASN77 4.7 11.4 1.0
C E:ASN76 4.8 8.7 1.0
CB E:LEU75 4.8 9.3 1.0
CA E:LEU82 4.8 8.2 1.0
O E:GLY80 4.8 9.5 1.0
C E:ALA74 4.9 7.9 1.0

Reference:

E.S.Radisky, D.E.Koshland Jr.. A Clogged Gutter Mechanism For Protease Inhibitors. Proc.Natl.Acad.Sci.Usa V. 99 10316 2002.
ISSN: ISSN 0027-8424
PubMed: 12142461
DOI: 10.1073/PNAS.112332899
Page generated: Mon Jul 7 17:02:26 2025

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