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Zinc in PDB 1c2e: Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases

Enzymatic activity of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases

All present enzymatic activity of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases:
3.4.21.4;

Protein crystallography data

The structure of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases, PDB code: 1c2e was solved by B.A.Katz, C.Luong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.50 / 1.65
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 54.970, 54.970, 109.760, 90.00, 90.00, 120.00
R / Rfree (%) 17.9 / 21.2

Other elements in 1c2e:

The structure of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases (pdb code 1c2e). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases, PDB code: 1c2e:

Zinc binding site 1 out of 1 in 1c2e

Go back to Zinc Binding Sites List in 1c2e
Zinc binding site 1 out of 1 in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn409

b:18.4
occ:1.00
 OG A:SER195 2.3 18.9 1.0
N3' A:BAK246 2.3 26.6 0.7
NE2 A:HIS57 2.3 11.9 1.0
N3 A:BAK246 2.3 17.9 1.0
HB3 A:SER195 2.6 18.9 1.0
CB A:SER195 2.9 16.9 1.0
H3' A:BAK246 3.0 30.4 0.7
CD2 A:HIS57 3.1 9.8 1.0
C4' A:BAK246 3.1 29.3 0.7
HD2 A:HIS57 3.2 8.6 1.0
H3 A:BAK246 3.3 15.7 1.0
C8' A:BAK246 3.3 28.0 0.7
C4 A:BAK246 3.3 19.6 1.0
C8 A:BAK246 3.3 23.7 1.0
CE1 A:HIS57 3.4 12.1 1.0
C3' A:BAK246 3.4 30.2 0.7
HA A:GLN192 3.5 22.8 1.0
O A:HOH337 3.5 19.1 1.0
C9 A:BAK246 3.6 27.6 1.0
H1 A:HOH337 3.6 23.1 1.0
C3 A:BAK246 3.7 16.4 1.0
HB2 A:SER195 3.7 17.7 1.0
HE1 A:HIS57 3.7 14.8 1.0
HA A:SER195 3.8 16.4 1.0
CA A:SER195 3.9 16.3 1.0
H A:GLY193 4.0 18.2 1.0
O A:SER214 4.1 10.5 1.0
C5' A:BAK246 4.2 30.7 0.7
H A:SER195 4.3 16.0 1.0
N4' A:BAK246 4.3 30.7 0.7
CG A:HIS57 4.3 10.3 1.0
H2 A:HOH337 4.4 21.5 1.0
ND1 A:HIS57 4.4 10.8 1.0
C5 A:BAK246 4.4 16.8 1.0
N4 A:BAK246 4.4 21.9 1.0
HB3 A:GLN192 4.5 30.6 1.0
CA A:GLN192 4.6 24.0 1.0
N A:SER195 4.6 16.9 1.0
C2' A:BAK246 4.7 31.3 0.7
O9 A:BAK246 4.8 28.1 1.0
N A:GLY193 4.9 19.3 1.0
CB A:GLN192 4.9 29.5 1.0
HG12 A:VAL213 5.0 12.6 1.0
HB2 A:GLN192 5.0 30.4 1.0

Reference:

B.A.Katz, J.M.Clark, J.S.Finer-Moore, T.E.Jenkins, C.R.Johnson, M.J.Ross, C.Luong, W.R.Moore, R.M.Stroud. Design of Potent Selective Zinc-Mediated Serine Protease Inhibitors. Nature V. 391 608 1998.
ISSN: ISSN 0028-0836
PubMed: 9468142
DOI: 10.1038/35422
Page generated: Sat Oct 12 22:53:08 2024

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