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Calcium in PDB 1smf: Studies on An Artificial Trypsin Inhibitor Peptide Derived From the Mung Bean Inhibitor

Enzymatic activity of Studies on An Artificial Trypsin Inhibitor Peptide Derived From the Mung Bean Inhibitor

All present enzymatic activity of Studies on An Artificial Trypsin Inhibitor Peptide Derived From the Mung Bean Inhibitor:
3.4.21.4;

Protein crystallography data

The structure of Studies on An Artificial Trypsin Inhibitor Peptide Derived From the Mung Bean Inhibitor, PDB code: 1smf was solved by Q.Huang, Y.Li, S.Zhang, S.Liu, Y.Tang, C.Qi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.230, 63.620, 69.540, 90.00, 90.00, 90.00
R / Rfree (%) 19 / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Studies on An Artificial Trypsin Inhibitor Peptide Derived From the Mung Bean Inhibitor (pdb code 1smf). 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 Studies on An Artificial Trypsin Inhibitor Peptide Derived From the Mung Bean Inhibitor, PDB code: 1smf:

Calcium binding site 1 out of 1 in 1smf

Go back to Calcium Binding Sites List in 1smf
Calcium binding site 1 out of 1 in the Studies on An Artificial Trypsin Inhibitor Peptide Derived From the Mung Bean Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Studies on An Artificial Trypsin Inhibitor Peptide Derived From the Mung Bean Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca0

b:9.9
occ:1.00
H2 E:HOH251 1.7 0.0 1.0
H1 E:HOH277 2.1 0.0 1.0
O E:VAL75 2.2 7.2 1.0
O E:HOH251 2.4 13.9 1.0
O E:ASN72 2.4 2.0 1.0
O E:HOH277 2.4 7.6 1.0
OE2 E:GLU80 2.5 9.6 1.0
OE1 E:GLU70 2.5 2.0 1.0
H1 E:HOH251 3.0 0.0 1.0
H2 E:HOH277 3.1 0.0 1.0
C E:VAL75 3.4 2.7 1.0
H E:GLU77 3.4 0.0 1.0
H E:VAL75 3.4 0.0 1.0
CD E:GLU70 3.5 8.0 1.0
CD E:GLU80 3.5 9.8 1.0
C E:ASN72 3.5 2.0 1.0
H E:ASP71 3.8 0.0 1.0
CG E:GLU80 3.8 12.7 1.0
OE2 E:GLU70 3.8 9.4 1.0
CA E:VAL76 4.0 5.9 1.0
N E:VAL76 4.1 2.0 1.0
N E:VAL75 4.1 3.9 1.0
N E:GLU77 4.2 6.4 1.0
H E:ASN72 4.2 0.0 1.0
CA E:ILE73 4.3 5.9 1.0
OE1 E:GLU77 4.3 14.2 1.0
CG E:GLU77 4.3 14.0 1.0
CA E:VAL75 4.4 3.4 1.0
N E:ILE73 4.4 3.2 1.0
N E:ASN72 4.4 2.5 1.0
C E:ILE73 4.5 8.6 1.0
CA E:ASN72 4.5 3.2 1.0
C E:VAL76 4.6 8.3 1.0
OE1 E:GLU80 4.6 12.8 1.0
CB E:ASN72 4.6 2.3 1.0
H1 E:HOH250 4.7 0.0 1.0
N E:ASP71 4.7 2.0 1.0
CD E:GLU77 4.8 13.2 1.0
O E:HOH309 4.8 10.9 1.0
CG E:GLU70 4.8 6.9 1.0
N E:ASN74 4.8 9.1 1.0
O E:ILE73 4.8 2.0 1.0
CB E:GLU77 4.9 3.4 1.0
CA E:GLU70 4.9 4.3 1.0
H E:ASN74 4.9 0.0 1.0
H2 E:HOH309 4.9 0.0 1.0
H E:VAL76 5.0 0.0 1.0

Reference:

Y.Li, Q.Huang, S.Zhang, S.Liu, C.Chi, Y.Tang. Studies on An Artificial Trypsin Inhibitor Peptide Derived From the Mung Bean Trypsin Inhibitor: Chemical Synthesis, Refolding, and Crystallographic Analysis of Its Complex with Trypsin. J.Biochem.(Tokyo) V. 116 18 1994.
ISSN: ISSN 0021-924X
PubMed: 7798176
Page generated: Thu Jul 11 22:43:53 2024

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