Chlorine in PDB 3wjz: Orotidine 5'-Monophosphate Decarboxylase D75N Mutant From M. Thermoautotrophicus Complexed with 6-Amino-Ump

Enzymatic activity of Orotidine 5'-Monophosphate Decarboxylase D75N Mutant From M. Thermoautotrophicus Complexed with 6-Amino-Ump

All present enzymatic activity of Orotidine 5'-Monophosphate Decarboxylase D75N Mutant From M. Thermoautotrophicus Complexed with 6-Amino-Ump:
4.1.1.23;

Protein crystallography data

The structure of Orotidine 5'-Monophosphate Decarboxylase D75N Mutant From M. Thermoautotrophicus Complexed with 6-Amino-Ump, PDB code: 3wjz was solved by M.Fujihashi, E.F.Pai, K.Miki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	50.00 / 1.39
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	58.067, 103.595, 73.705, 90.00, 90.00, 90.00
*R / R_free (%)*	15.7 / 17.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Orotidine 5'-Monophosphate Decarboxylase D75N Mutant From M. Thermoautotrophicus Complexed with 6-Amino-Ump (pdb code 3wjz). 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 Orotidine 5'-Monophosphate Decarboxylase D75N Mutant From M. Thermoautotrophicus Complexed with 6-Amino-Ump, PDB code: 3wjz:

Chlorine binding site 1 out of 1 in 3wjz

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Chlorine Binding Sites List in 3wjz

Chlorine binding site 1 out of 1 in the Orotidine 5'-Monophosphate Decarboxylase D75N Mutant From M. Thermoautotrophicus Complexed with 6-Amino-Ump

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Orotidine 5'-Monophosphate Decarboxylase D75N Mutant From M. Thermoautotrophicus Complexed with 6-Amino-Ump within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl302 b:11.8 occ:0.50	O2'	A:NUP301	3.1	9.9	1.0
	C6	A:NUP301	3.2	10.0	1.0
	NZ	A:LYS72	3.2	13.3	0.5
	N1	A:NUP301	3.2	8.4	1.0
	CE	A:LYS72	3.4	13.8	0.5
	C5	A:NUP301	3.6	10.3	1.0
	N3	A:NUP301	3.6	12.3	1.0
	C2'	A:NUP301	3.6	9.1	1.0
	CE	A:LYS72	3.6	12.0	0.5
	C2	A:NUP301	3.7	8.2	1.0
	C1'	A:NUP301	3.7	8.6	1.0
	CE	A:MET126	3.9	13.2	1.0
	C4	A:NUP301	4.0	9.2	1.0
	N2	A:NUP301	4.1	8.7	1.0
	CD	A:LYS72	4.3	14.4	0.5
	NZ	A:LYS72	4.3	13.1	0.5
	O2	A:NUP301	4.4	9.3	1.0
	OD2	A:ASP70	4.5	11.8	1.0
	CG	A:LYS72	4.6	12.4	0.5
	O4	A:NUP301	4.9	10.1	1.0

Reference:

M.Fujihashi, T.Ishida, S.Kuroda, L.P.Kotra, E.F.Pai, K.Miki. Substrate Distortion Contributes to the Catalysis of Orotidine 5'-Monophosphate Decarboxylase. J.Am.Chem.Soc. V. 135 17432 2013.
ISSN: ISSN 0002-7863
PubMed: 24151964
DOI: 10.1021/JA408197K

Page generated: Sat Dec 12 10:19:23 2020

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