Calcium in PDB 1htd: Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Ht-D)

Enzymatic activity of Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Ht-D)

All present enzymatic activity of Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Ht-D):
3.4.24.42;

Protein crystallography data

The structure of Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Ht-D), PDB code: 1htd was solved by D.Zhang, I.Botos, F.-X.Gomis-Rueth, R.Doll, C.Blood, F.G.Njoroge, J.W.Fox, W.Bode, E.F.Meyer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	25.00 / 2.10
*Space group*	P 6₅
*Cell size a, b, c (Å), α, β, γ (°)*	97.320, 97.320, 87.760, 90.00, 90.00, 120.00
*R / R_free (%)*	18 / n/a

Other elements in 1htd:

The structure of Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Ht-D) also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Ht-D) (pdb code 1htd). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Ht-D), PDB code: 1htd:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1htd

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Calcium Binding Sites List in 1htd

Calcium binding site 1 out of 2 in the Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Ht-D)

Mono view

Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Ht-D) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Ca403 b:18.9 occ:1.00	O	A:HOH430	1.8	31.2	1.0
	O	A:HOH416	1.8	33.4	1.0
	O	A:CYS197	2.2	27.2	1.0
	OE1	A:GLU9	2.3	36.6	1.0
	OD1	A:ASP93	2.4	27.1	1.0
	OD2	A:ASP93	2.5	34.3	1.0
	OD1	A:ASN200	2.5	25.3	1.0
	CG	A:ASP93	2.8	14.5	1.0
	C	A:CYS197	3.4	11.5	1.0
	CD	A:GLU9	3.4	6.5	1.0
	CG	A:ASN200	3.6	15.2	1.0
	CG	A:GLU9	4.0	5.0	1.0
	O	A:HOH454	4.0	38.4	1.0
	CA	A:CYS197	4.1	14.1	1.0
	ND2	A:ASN200	4.2	16.1	1.0
	CB	A:ASP93	4.4	25.1	1.0
	N	A:ILE198	4.4	26.0	1.0
	CB	A:CYS197	4.4	20.4	1.0
	O	A:TYR7	4.4	18.8	1.0
	OE2	A:GLU9	4.5	60.6	1.0
	CB	A:GLU9	4.5	15.4	1.0
	CA	A:ILE198	4.5	14.3	1.0
	O	A:ASN200	4.6	29.6	1.0
	CB	A:ASN200	4.9	5.5	1.0
	N	A:ASN200	4.9	26.3	1.0
	N	A:GLU9	4.9	26.5	1.0
	SG	A:CYS197	4.9	22.7	1.0

Calcium binding site 2 out of 2 in 1htd

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Calcium Binding Sites List in 1htd

Calcium binding site 2 out of 2 in the Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Ht-D)

Mono view

Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Ht-D) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Ca404 b:24.1 occ:1.00	O	B:HOH349	1.8	26.0	1.0
	O	B:CYS197	2.3	26.4	1.0
	OD1	B:ASN200	2.3	22.7	1.0
	OE1	B:GLU9	2.4	29.8	1.0
	OD1	B:ASP93	2.4	30.5	1.0
	OD2	B:ASP93	2.5	20.0	1.0
	O	B:HOH357	2.7	34.7	1.0
	CG	B:ASP93	2.9	30.3	1.0
	CG	B:ASN200	3.4	23.3	1.0
	C	B:CYS197	3.5	14.6	1.0
	CD	B:GLU9	3.5	9.8	1.0
	ND2	B:ASN200	3.9	17.9	1.0
	CG	B:GLU9	4.0	16.9	1.0
	CA	B:CYS197	4.2	9.6	1.0
	O	B:TYR7	4.4	27.1	1.0
	CB	B:CYS197	4.4	9.3	1.0
	CB	B:ASP93	4.4	24.0	1.0
	N	B:ILE198	4.4	18.3	1.0
	CB	B:GLU9	4.4	18.3	1.0
	CA	B:ILE198	4.5	12.3	1.0
	O	B:HOH333	4.5	39.7	1.0
	OE2	B:GLU9	4.5	28.7	1.0
	O	B:ASN200	4.6	20.0	1.0
	O	B:HOH321	4.6	26.5	1.0
	CB	B:ASN200	4.7	8.7	1.0
	O	B:HOH332	4.8	24.5	1.0
	N	B:GLU9	4.8	32.9	1.0
	N	B:ASN200	4.9	18.2	1.0
	SG	B:CYS197	4.9	16.0	1.0
	N	B:LEU199	5.0	22.7	1.0

Reference:

D.Zhang, I.Botos, F.X.Gomis-Ruth, R.Doll, C.Blood, F.G.Njoroge, J.W.Fox, W.Bode, E.F.Meyer. Structural Interaction of Natural and Synthetic Inhibitors with the Venom Metalloproteinase, Atrolysin C (Form D). Proc.Natl.Acad.Sci.Usa V. 91 8447 1994.
ISSN: ISSN 0027-8424
PubMed: 8078901
DOI: 10.1073/PNAS.91.18.8447

Page generated: Mon Jul 7 15:41:40 2025

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