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Zinc in PDB 3kwd: Inactive Truncation of the Beta-Carboxysomal Gamma-Carbonic Anhydrase, Ccmm, Form 1

Enzymatic activity of Inactive Truncation of the Beta-Carboxysomal Gamma-Carbonic Anhydrase, Ccmm, Form 1

All present enzymatic activity of Inactive Truncation of the Beta-Carboxysomal Gamma-Carbonic Anhydrase, Ccmm, Form 1:
4.2.1.1;

Protein crystallography data

The structure of Inactive Truncation of the Beta-Carboxysomal Gamma-Carbonic Anhydrase, Ccmm, Form 1, PDB code: 3kwd was solved by K.L.Pena, M.S.Kimber, S.E.Castel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	26.97 / 1.10
*Space group*	H 3
*Cell size a, b, c (Å), α, β, γ (°)*	103.006, 103.006, 44.953, 90.00, 90.00, 120.00
*R / R_free (%)*	13.3 / 14.8

Other elements in 3kwd:

The structure of Inactive Truncation of the Beta-Carboxysomal Gamma-Carbonic Anhydrase, Ccmm, Form 1 also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Inactive Truncation of the Beta-Carboxysomal Gamma-Carbonic Anhydrase, Ccmm, Form 1 (pdb code 3kwd). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Inactive Truncation of the Beta-Carboxysomal Gamma-Carbonic Anhydrase, Ccmm, Form 1, PDB code: 3kwd:

Zinc binding site 1 out of 1 in 3kwd

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Zinc Binding Sites List in 3kwd

Zinc binding site 1 out of 1 in the Inactive Truncation of the Beta-Carboxysomal Gamma-Carbonic Anhydrase, Ccmm, Form 1

Mono view

Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Inactive Truncation of the Beta-Carboxysomal Gamma-Carbonic Anhydrase, Ccmm, Form 1 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Zn194 b:9.1 occ:1.00	NE2	A:HIS107	2.2	10.0	1.0
	O	A:HOH336	2.2	8.6	1.0
	O	A:HOH249	2.2	10.9	1.0
	ND1	A:HIS75	2.2	10.2	1.0
	O	A:HOH337	2.2	9.1	1.0
	CE1	A:HIS75	3.1	10.6	1.0
	CE1	A:HIS107	3.1	9.9	1.0
	CD2	A:HIS107	3.2	10.1	1.0
	CG	A:HIS75	3.3	10.2	1.0
	CB	A:HIS75	3.7	10.3	1.0
	O	A:HOH338	4.1	15.7	1.0
	O	A:HOH339	4.2	21.1	1.0
	NE2	A:HIS75	4.3	11.4	1.0
	ND1	A:HIS107	4.3	10.6	1.0
	CG	A:HIS107	4.3	10.4	1.0
	CD2	A:HIS75	4.4	11.4	1.0
	O	A:GLY76	4.5	11.4	1.0
	N	A:GLY76	4.6	10.3	1.0
	OE1	A:GLU56	4.6	15.1	1.0
	C	A:GLY76	4.8	10.1	1.0
	C	A:HIS75	4.9	10.1	1.0
	CA	A:HIS75	4.9	10.4	1.0

Reference:

K.L.Pena, S.E.Castel, C.De Araujo, G.S.Espie, M.S.Kimber. Structural Basis of the Oxidative Activation of the Carboxysomal {Gamma}-Carbonic Anhydrase, Ccmm. Proc.Natl.Acad.Sci.Usa V. 107 2455 2010.
ISSN: ISSN 0027-8424
PubMed: 20133749
DOI: 10.1073/PNAS.0910866107

Page generated: Wed Aug 20 11:08:26 2025

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