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Chlorine in PDB 1c2i: 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: 1c2i 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 / 1.47
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 55.000, 55.000, 109.760, 90.00, 90.00, 120.00
R / Rfree (%) 17.7 / 20.8

Other elements in 1c2i:

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

Calcium (Ca) 1 atom
Zinc (Zn) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases (pdb code 1c2i). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases, PDB code: 1c2i:

Chlorine binding site 1 out of 1 in 1c2i

Go back to Chlorine Binding Sites List in 1c2i
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl299

b:41.1
occ:1.00
 H1 A:HOH296 1.4 46.2 1.0
H2 A:HOH271 1.4 23.3 1.0
H2 A:HOH377 2.1 48.7 1.0
O A:HOH296 2.4 48.5 1.0
H1 A:HOH271 2.4 22.5 1.0
O A:HOH271 2.5 19.5 1.0
H2 A:HOH296 2.5 47.8 1.0
HG21 A:VAL76 3.0 21.3 1.0
O A:HOH377 3.0 48.3 1.0
HG22 A:VAL76 3.3 20.4 1.0
HH11 A:ARG66 3.3 16.4 1.0
O A:ILE73 3.5 16.7 1.0
HA A:ASN74 3.6 16.9 1.0
H1 A:HOH377 3.6 46.4 1.0
CG2 A:VAL76 3.7 20.5 1.0
HZ A:PHE82 3.7 24.9 1.0
C A:ASN74 3.7 16.5 1.0
H1 A:HOH268 3.7 15.1 1.0
H2 A:HOH268 3.7 16.1 1.0
N A:VAL75 3.8 15.8 1.0
HH12 A:ARG66 3.9 16.8 1.0
O A:ASN74 4.0 20.8 1.0
C A:VAL75 4.0 15.9 1.0
NH1 A:ARG66 4.0 16.5 1.0
H1 A:HOH287 4.0 33.6 1.0
N A:VAL76 4.0 16.2 1.0
H A:VAL75 4.1 16.4 1.0
C A:ILE73 4.1 15.8 1.0
CA A:ASN74 4.1 16.1 1.0
O A:HOH268 4.1 14.8 1.0
HA A:VAL75 4.1 16.2 1.0
H A:VAL76 4.2 17.8 1.0
HA A:VAL76 4.2 20.5 1.0
CA A:VAL75 4.2 15.6 1.0
HG23 A:VAL76 4.3 21.7 1.0
O A:VAL75 4.3 16.0 1.0
H2 A:HOH564 4.4 45.1 1.0
N A:ASN74 4.4 15.5 1.0
CA A:CA247 4.5 29.9 1.0
HE1 A:PHE82 4.5 23.7 1.0
CA A:VAL76 4.6 20.5 1.0
CZ A:PHE82 4.6 24.1 1.0
OE2 A:GLU70 4.7 19.5 1.0
HA A:ILE73 4.8 16.9 1.0
O A:HOH564 4.8 45.5 1.0
CB A:VAL76 4.8 21.8 1.0
CE1 A:PHE82 5.0 23.8 1.0
O A:HOH287 5.0 35.0 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: Thu Jul 10 16:24:09 2025

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