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Zinc in PDB 1ghy: A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site
Enzymatic activity of A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site
All present enzymatic activity of A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site:
3.4.21.5;
3.4.21.5;
Protein crystallography data
The structure of A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site, PDB code: 1ghy
was solved by
B.A.Katz,
K.Elrod,
C.Luong,
M.Rice,
R.L.Mackman,
P.A.Sprengeler,
J.Spencer,
J.Hatayte,
J.Janc,
J.Link,
J.Litvak,
R.Rai,
K.Rice,
S.Sideris,
E.Verner,
W.Young,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 7.00 / 1.85 |
| Space group | C 1 2 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 71.890, 72.220, 72.740, 90.00, 100.97, 90.00 |
| R / Rfree (%) | 19.5 / 22 |
Other elements in 1ghy:
The structure of A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site also contains other interesting chemical elements:
| Calcium | (Ca) | 1 atom |
| Sodium | (Na) | 1 atom |
Zinc Binding Sites:
The binding sites of Zinc atom in the A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site
(pdb code 1ghy). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site, PDB code: 1ghy:
Jump to Zinc binding site number: 1; 2; 3;
In total 3 binding sites of Zinc where determined in the A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site, PDB code: 1ghy:
Jump to Zinc binding site number: 1; 2; 3;
Zinc binding site 1 out of 3 in 1ghy
Go back to
Zinc Binding Sites List in 1ghy
Zinc binding site 1 out
of 3 in the A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site within 5.0Å range:
|
Zinc binding site 2 out of 3 in 1ghy
Go back to
Zinc Binding Sites List in 1ghy
Zinc binding site 2 out
of 3 in the A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site within 5.0Å range:
|
Zinc binding site 3 out of 3 in 1ghy
Go back to
Zinc Binding Sites List in 1ghy
Zinc binding site 3 out
of 3 in the A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site within 5.0Å range:
|
Reference:
B.A.Katz,
K.Elrod,
C.Luong,
M.J.Rice,
R.L.Mackman,
P.A.Sprengeler,
J.Spencer,
J.Hataye,
J.Janc,
J.Link,
J.Litvak,
R.Rai,
K.Rice,
S.Sideris,
E.Verner,
W.Young.
A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site. J.Mol.Biol. V. 307 1451 2001.
ISSN: ISSN 0022-2836
PubMed: 11292354
DOI: 10.1006/JMBI.2001.4516
Page generated: Sun Oct 13 01:31:21 2024
ISSN: ISSN 0022-2836
PubMed: 11292354
DOI: 10.1006/JMBI.2001.4516
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