Chlorine in PDB 5lkt: Crystal Structure of the P300 Acetyltransferase Catalytic Core with Butyryl-Coenzyme A.

Enzymatic activity of Crystal Structure of the P300 Acetyltransferase Catalytic Core with Butyryl-Coenzyme A.

All present enzymatic activity of Crystal Structure of the P300 Acetyltransferase Catalytic Core with Butyryl-Coenzyme A.:
2.3.1.48;

Protein crystallography data

The structure of Crystal Structure of the P300 Acetyltransferase Catalytic Core with Butyryl-Coenzyme A., PDB code: 5lkt was solved by Z.Kaczmarska, E.Ortega, J.A.Marquez, D.Panne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	50.01 / 2.04
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	92.480, 154.690, 109.230, 90.00, 90.00, 90.00
*R / R_free (%)*	17.7 / 20.4

Other elements in 5lkt:

The structure of Crystal Structure of the P300 Acetyltransferase Catalytic Core with Butyryl-Coenzyme A. also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the P300 Acetyltransferase Catalytic Core with Butyryl-Coenzyme A. (pdb code 5lkt). 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 P300 Acetyltransferase Catalytic Core with Butyryl-Coenzyme A., PDB code: 5lkt:

Chlorine binding site 1 out of 1 in 5lkt

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Chlorine Binding Sites List in 5lkt

Chlorine binding site 1 out of 1 in the Crystal Structure of the P300 Acetyltransferase Catalytic Core with Butyryl-Coenzyme A.

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 P300 Acetyltransferase Catalytic Core with Butyryl-Coenzyme A. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl1710 b:60.2 occ:1.00	O	A:HOH1999	3.6	41.2	1.0
	SG	A:CYS1653	4.0	29.4	1.0
	O	A:HOH1827	4.3	43.8	1.0
	CB	A:LYS1637	4.3	33.6	1.0
	CZ2	A:TRP1649	4.3	30.5	1.0
	CD	A:LYS1637	4.3	40.1	1.0
	CD2	A:LEU1639	4.4	32.0	1.0
	O	A:LYS1637	4.4	30.0	1.0
	O	A:HOH2081	4.6	58.2	1.0
	O	A:HOH1988	4.7	38.3	1.0
	NE1	A:TRP1649	4.8	29.5	1.0
	CG	A:LYS1637	4.8	36.7	1.0
	CE2	A:TRP1649	4.9	28.7	1.0
	CB	A:CYS1653	4.9	28.3	1.0
	O	A:HOH2155	4.9	62.3	1.0

Reference:

Z.Kaczmarska, E.Ortega, A.Goudarzi, H.Huang, S.Kim, J.A.Marquez, Y.Zhao, S.Khochbin, D.Panne. Structure of P300 in Complex with Acyl-Coa Variants. Nat. Chem. Biol. V. 13 21 2017.
ISSN: ESSN 1552-4469
PubMed: 27820805
DOI: 10.1038/NCHEMBIO.2217

Page generated: Sat Dec 12 12:03:20 2020

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