Chlorine in PDB 1kxh: Crystal Structure of the Complex Between An Inactive Mutant of Psychrophilic Alpha-Amylase (D174N) and Acarbose

Enzymatic activity of Crystal Structure of the Complex Between An Inactive Mutant of Psychrophilic Alpha-Amylase (D174N) and Acarbose

All present enzymatic activity of Crystal Structure of the Complex Between An Inactive Mutant of Psychrophilic Alpha-Amylase (D174N) and Acarbose:
3.2.1.1;

Protein crystallography data

The structure of Crystal Structure of the Complex Between An Inactive Mutant of Psychrophilic Alpha-Amylase (D174N) and Acarbose, PDB code: 1kxh was solved by N.Aghajari, R.Haser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	27.70 / 2.30
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	71.100, 139.900, 115.300, 90.00, 90.00, 90.00
*R / R_free (%)*	13.8 / 18.8

Other elements in 1kxh:

The structure of Crystal Structure of the Complex Between An Inactive Mutant of Psychrophilic Alpha-Amylase (D174N) and Acarbose also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Complex Between An Inactive Mutant of Psychrophilic Alpha-Amylase (D174N) and Acarbose (pdb code 1kxh). 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 the Complex Between An Inactive Mutant of Psychrophilic Alpha-Amylase (D174N) and Acarbose, PDB code: 1kxh:

Chlorine binding site 1 out of 1 in 1kxh

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Chlorine Binding Sites List in 1kxh

Chlorine binding site 1 out of 1 in the Crystal Structure of the Complex Between An Inactive Mutant of Psychrophilic Alpha-Amylase (D174N) and Acarbose

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 the Complex Between An Inactive Mutant of Psychrophilic Alpha-Amylase (D174N) and Acarbose within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl900 b:17.2 occ:1.00	NZ	A:LYS300	3.2	17.5	1.0
	NE	A:ARG172	3.3	14.2	1.0
	NH1	A:ARG172	3.4	17.3	1.0
	O	A:HOH1003	3.5	14.4	1.0
	ND2	A:ASN262	3.5	13.0	1.0
	CE	A:LYS300	3.7	13.0	1.0
	CZ	A:ARG172	3.7	16.9	1.0
	CG2	A:THR221	3.8	7.9	1.0
	CE2	A:PHE259	4.2	9.6	1.0
	CD	A:ARG172	4.4	12.6	1.0
	CE1	A:PHE198	4.4	11.2	1.0
	CB	A:ASN262	4.5	10.7	1.0
	CG	A:ASN262	4.5	12.1	1.0
	CZ	A:PHE259	4.6	11.8	1.0
	CG	A:GLU200	4.7	14.2	1.0
	CB	A:THR221	4.7	11.8	1.0
	CZ	A:PHE223	4.8	9.5	1.0
	O	A:HOH1004	4.8	13.4	1.0
	CD2	A:PHE259	4.8	8.8	1.0
	O	A:HOH1002	4.9	16.3	1.0
	OE1	A:GLN33	4.9	15.3	1.0
	CB	A:GLU200	4.9	14.0	1.0

Reference:

N.Aghajari, M.Roth, R.Haser. Crystallographic Evidence of A Transglycosylation Reaction: Ternary Complexes of A Psychrophilic Alpha-Amylase. Biochemistry V. 41 4273.
ISSN: ISSN 0006-2960
PubMed: 11914073
DOI: 10.1021/BI0160516

Page generated: Thu Jul 10 17:53:46 2025

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