Chlorine in PDB 5vzc: Post-Catalytic Complex of Human Polymerase Mu (G433S) Mutant with Incoming Dttp

Enzymatic activity of Post-Catalytic Complex of Human Polymerase Mu (G433S) Mutant with Incoming Dttp

All present enzymatic activity of Post-Catalytic Complex of Human Polymerase Mu (G433S) Mutant with Incoming Dttp:
2.7.7.7;

Protein crystallography data

The structure of Post-Catalytic Complex of Human Polymerase Mu (G433S) Mutant with Incoming Dttp, PDB code: 5vzc was solved by A.F.Moon, J.M.Pryor, D.A.Ramsden, T.A.Kunkel, K.Bebenek, L.C.Pedersen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	32.82 / 1.55
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	60.112, 68.716, 110.993, 90.00, 90.00, 90.00
*R / R_free (%)*	16.5 / 19

Other elements in 5vzc:

The structure of Post-Catalytic Complex of Human Polymerase Mu (G433S) Mutant with Incoming Dttp also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Sodium	(Na)	2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Post-Catalytic Complex of Human Polymerase Mu (G433S) Mutant with Incoming Dttp (pdb code 5vzc). 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 Post-Catalytic Complex of Human Polymerase Mu (G433S) Mutant with Incoming Dttp, PDB code: 5vzc:

Chlorine binding site 1 out of 1 in 5vzc

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Chlorine Binding Sites List in 5vzc

Chlorine binding site 1 out of 1 in the Post-Catalytic Complex of Human Polymerase Mu (G433S) Mutant with Incoming Dttp

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Post-Catalytic Complex of Human Polymerase Mu (G433S) Mutant with Incoming Dttp within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl502 b:18.5 occ:0.72	N	A:SER458	3.1	10.3	1.0
	O1	A:EDO506	3.3	39.1	1.0
	OG	A:SER458	3.3	14.9	1.0
	O4'	T:DA7	3.4	21.1	1.0
	C4'	T:DA7	3.5	21.7	1.0
	NH2	A:ARG445	3.5	10.9	1.0
	CB	A:SER458	3.6	13.8	1.0
	CB	A:ASN457	3.6	10.4	1.0
	C1'	T:DA7	3.6	22.3	1.0
	NH1	A:ARG445	3.6	12.6	1.0
	CZ	A:ARG445	3.9	8.4	1.0
	CA	A:SER458	3.9	9.6	1.0
	O2	T:DT6	4.0	13.8	1.0
	CA	A:ASN457	4.0	9.3	1.0
	C	A:ASN457	4.0	10.1	1.0
	C5'	T:DA7	4.2	31.9	1.0
	O2	A:EDO506	4.3	26.9	1.0
	C2'	T:DA7	4.4	26.6	1.0
	CG	A:ASN457	4.5	12.8	1.0
	C1'	T:DT6	4.5	16.9	1.0
	NH2	A:ARG387	4.5	19.0	1.0
	C1	A:EDO506	4.6	38.4	1.0
	C3'	T:DA7	4.6	21.4	1.0
	O3'	T:DT6	4.7	14.6	1.0
	N9	T:DA7	4.7	16.9	1.0
	OG	A:SER433	4.8	8.4	0.4
	C4'	T:DT6	4.9	10.9	1.0
	O5'	T:DA7	5.0	29.6	1.0
	C	A:SER458	5.0	9.7	1.0

Reference:

A.F.Moon, J.M.Pryor, D.A.Ramsden, T.A.Kunkel, K.Bebenek, L.C.Pedersen. Structural Accommodation of Ribonucleotide Incorporation By the Dna Repair Enzyme Polymerase Mu. Nucleic Acids Res. V. 45 9138 2017.
ISSN: ESSN 1362-4962
PubMed: 28911097
DOI: 10.1093/NAR/GKX527

Page generated: Fri Jul 26 19:07:47 2024

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