Calcium in PDB 1jd7: Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase

Enzymatic activity of Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase

All present enzymatic activity of Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase:
3.2.1.1;

Protein crystallography data

The structure of Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase, PDB code: 1jd7 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)*	25.70 / 2.25
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	70.300, 136.400, 113.500, 90.00, 90.00, 90.00
*R / R_free (%)*	17.9 / 21.5

Other elements in 1jd7:

The structure of Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase (pdb code 1jd7). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase, PDB code: 1jd7:

Calcium binding site 1 out of 1 in 1jd7

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Calcium Binding Sites List in 1jd7

Calcium binding site 1 out of 1 in the Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase

Mono view

Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure Analysis of the Mutant K300R of Pseudoalteromonas Haloplanctis Alpha-Amylase within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Ca800 b:7.5 occ:1.00	O	A:HOH1091	2.4	1.1	1.0
	O	A:HIS178	2.4	11.1	1.0
	OD1	A:ASN88	2.4	10.2	1.0
	O	A:HOH1108	2.4	9.6	1.0
	O	A:HOH1107	2.4	3.3	1.0
	OD1	A:ASP144	2.5	13.2	1.0
	OD2	A:ASP144	2.6	13.6	1.0
	O	A:GLN135	2.7	11.2	1.0
	CG	A:ASP144	2.9	12.4	1.0
	C	A:GLN135	3.4	11.0	1.0
	CG	A:ASN88	3.5	12.6	1.0
	C	A:HIS178	3.5	9.2	1.0
	CA	A:GLN135	4.0	10.6	1.0
	ND2	A:ASN88	4.1	10.6	1.0
	CB	A:HIS178	4.2	7.8	1.0
	O	A:ASN88	4.3	13.8	1.0
	CG2	A:VAL179	4.3	8.2	1.0
	N	A:ASN136	4.3	11.0	1.0
	CB	A:ASP144	4.4	10.3	1.0
	CA	A:HIS178	4.4	9.1	1.0
	ND1	A:HIS117	4.4	11.9	1.0
	N	A:VAL179	4.4	9.1	1.0
	CE1	A:HIS117	4.5	13.2	1.0
	CA	A:VAL179	4.5	8.9	1.0
	O	A:LEU145	4.5	13.1	1.0
	CA	A:ASN136	4.6	12.2	1.0
	CB	A:ASN88	4.7	10.2	1.0
	CB	A:GLN135	4.7	8.7	1.0
	O	A:VAL134	4.8	8.9	1.0
	O	A:CYS137	4.8	11.5	1.0
	O	A:HOH1144	4.9	6.3	1.0

Reference:

N.Aghajari, G.Feller, C.Gerday, R.Haser. Structural Basis of Alpha-Amylase Activation By Chloride Protein Sci. V. 11 1435 2002.
ISSN: ISSN 0961-8368
PubMed: 12021442
DOI: 10.1110/PS.0202602

Page generated: Thu Jul 11 10:42:33 2024

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