Calcium in PDB 1ht3: Mercury Induced Modifications in the Stereochemistry of the Active Site Through Cys-73 in A Serine Protease: Crystal Structure of the Complex of A Partially Modified Proteinase K with Mercury at 1.8 A Resolution

Enzymatic activity of Mercury Induced Modifications in the Stereochemistry of the Active Site Through Cys-73 in A Serine Protease: Crystal Structure of the Complex of A Partially Modified Proteinase K with Mercury at 1.8 A Resolution

All present enzymatic activity of Mercury Induced Modifications in the Stereochemistry of the Active Site Through Cys-73 in A Serine Protease: Crystal Structure of the Complex of A Partially Modified Proteinase K with Mercury at 1.8 A Resolution:
3.4.21.64;

Protein crystallography data

The structure of Mercury Induced Modifications in the Stereochemistry of the Active Site Through Cys-73 in A Serine Protease: Crystal Structure of the Complex of A Partially Modified Proteinase K with Mercury at 1.8 A Resolution, PDB code: 1ht3 was solved by S.Gourinath, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	10.00 / 1.80
*Space group*	P 4₃ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	68.360, 68.360, 108.700, 90.00, 90.00, 90.00
*R / R_free (%)*	16.4 / 22.1

Other elements in 1ht3:

The structure of Mercury Induced Modifications in the Stereochemistry of the Active Site Through Cys-73 in A Serine Protease: Crystal Structure of the Complex of A Partially Modified Proteinase K with Mercury at 1.8 A Resolution also contains other interesting chemical elements:

Mercury

(Hg)

2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Mercury Induced Modifications in the Stereochemistry of the Active Site Through Cys-73 in A Serine Protease: Crystal Structure of the Complex of A Partially Modified Proteinase K with Mercury at 1.8 A Resolution (pdb code 1ht3). 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 Mercury Induced Modifications in the Stereochemistry of the Active Site Through Cys-73 in A Serine Protease: Crystal Structure of the Complex of A Partially Modified Proteinase K with Mercury at 1.8 A Resolution, PDB code: 1ht3:

Calcium binding site 1 out of 1 in 1ht3

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Calcium Binding Sites List in 1ht3

Calcium binding site 1 out of 1 in the Mercury Induced Modifications in the Stereochemistry of the Active Site Through Cys-73 in A Serine Protease: Crystal Structure of the Complex of A Partially Modified Proteinase K with Mercury at 1.8 A Resolution

Mono view

Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Mercury Induced Modifications in the Stereochemistry of the Active Site Through Cys-73 in A Serine Protease: Crystal Structure of the Complex of A Partially Modified Proteinase K with Mercury at 1.8 A Resolution within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Ca282 b:9.9 occ:1.00	O	A:PRO175	2.4	8.3	1.0
	O	A:VAL177	2.4	9.2	1.0
	O	A:HOH502	2.5	15.1	1.0
	OD2	A:ASP200	2.5	9.1	1.0
	O	A:HOH504	2.5	9.6	1.0
	O	A:HOH501	2.6	12.3	1.0
	O	A:HOH503	2.7	10.8	1.0
	OD1	A:ASP200	2.8	11.4	1.0
	CG	A:ASP200	3.0	12.1	1.0
	C	A:PRO175	3.4	10.9	1.0
	C	A:VAL177	3.7	11.2	1.0
	CA	A:PRO175	4.1	10.4	1.0
	N	A:VAL177	4.2	11.9	1.0
	O	A:VAL198	4.4	13.5	1.0
	C	A:SER176	4.4	9.9	1.0
	N	A:SER176	4.4	7.9	1.0
	O	A:HOH607	4.4	65.5	1.0
	CB	A:ASP200	4.5	8.4	1.0
	O	A:GLU174	4.5	10.5	1.0
	CA	A:VAL177	4.6	10.5	1.0
	CA	A:CYS178	4.6	8.0	1.0
	N	A:CYS178	4.6	9.8	1.0
	N	A:THR179	4.7	8.1	1.0
	O	A:HOH655	4.7	42.8	1.0
	O	A:HOH722	4.7	40.0	1.0
	O	A:HOH514	4.7	17.2	1.0
	CA	A:SER176	4.7	8.4	1.0
	OG1	A:THR179	4.8	10.0	1.0
	SG	A:CYS249	5.0	10.4	1.0

Reference:

S.Gourinath, M.Degenhardt, S.Eschenburg, K.Moore, L.J.Delucas, C.H.Betzel, T.P.Singh. Mercury Induced Modifications in the Stereochemistry of the Active Site Through Cys-73 in A Serine Protease--Crystal Structure of the Complex of A Partially Modified Proteinase K with Mercury at 1.8 A Resolution Indian J.Biochem.Biophys. V. 38 298 2001.
ISSN: ISSN 0301-1208
PubMed: 11886076

Page generated: Thu Jul 11 10:08:26 2024

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