Chlorine in PDB 1sc1: Crystal Structure of An Active-Site Ligand-Free Form of the Human Caspase-1 C285A Mutant

Enzymatic activity of Crystal Structure of An Active-Site Ligand-Free Form of the Human Caspase-1 C285A Mutant

All present enzymatic activity of Crystal Structure of An Active-Site Ligand-Free Form of the Human Caspase-1 C285A Mutant:
3.4.22.36;

Protein crystallography data

The structure of Crystal Structure of An Active-Site Ligand-Free Form of the Human Caspase-1 C285A Mutant, PDB code: 1sc1 was solved by M.J.Romanowski, J.M.Scheer, T.O'brien, R.S.Mcdowell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	20.00 / 2.60
*Space group*	P 3₂ 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	71.782, 71.782, 118.451, 90.00, 90.00, 120.00
*R / R_free (%)*	23.1 / 27.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of An Active-Site Ligand-Free Form of the Human Caspase-1 C285A Mutant (pdb code 1sc1). 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 Crystal Structure of An Active-Site Ligand-Free Form of the Human Caspase-1 C285A Mutant, PDB code: 1sc1:

Chlorine binding site 1 out of 1 in 1sc1

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Chlorine Binding Sites List in 1sc1

Chlorine binding site 1 out of 1 in the Crystal Structure of An Active-Site Ligand-Free Form of the Human Caspase-1 C285A Mutant

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of An Active-Site Ligand-Free Form of the Human Caspase-1 C285A Mutant within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Cl1 b:33.2 occ:1.00	N	B:TRP340	3.0	76.9	1.0
	OG	B:SER339	3.0	76.5	1.0
	CB	B:TRP340	3.5	76.2	1.0
	NE	B:ARG341	3.7	77.8	1.0
	CA	B:TRP340	3.7	75.9	1.0
	N	B:ARG341	3.7	76.1	1.0
	C	B:SER339	3.9	77.7	1.0
	CA	B:SER339	3.9	78.9	1.0
	CG	B:ARG341	3.9	79.3	1.0
	CD	B:ARG341	4.0	78.6	1.0
	CB	B:SER339	4.0	78.2	1.0
	C	B:TRP340	4.3	75.4	1.0
	CZ	B:ARG341	4.7	77.1	1.0
	CG	B:TRP340	4.8	76.5	1.0
	CA	B:ARG341	4.9	78.7	1.0
	O	B:ARG341	4.9	80.9	1.0
	NH2	B:ARG341	4.9	77.0	1.0
	O	B:SER339	5.0	76.7	1.0
	CB	B:ARG341	5.0	79.1	1.0

Reference:

M.J.Romanowski, J.M.Scheer, T.O'brien, R.S.Mcdowell. Crystal Structures of A Ligand-Free and Malonate-Bound Human Caspase-1: Implications For the Mechanism of Substrate Binding. Structure V. 12 1361 2004.
ISSN: ISSN 0969-2126
PubMed: 15296730
DOI: 10.1016/J.STR.2004.05.010

Page generated: Thu Jul 10 19:24:05 2025

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