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Chlorine in PDB 5vz9: Post-Catalytic Complex of Human Polymerase Mu (G433A) Mutant with Incoming Dttp

Enzymatic activity of Post-Catalytic Complex of Human Polymerase Mu (G433A) Mutant with Incoming Dttp

All present enzymatic activity of Post-Catalytic Complex of Human Polymerase Mu (G433A) Mutant with Incoming Dttp:
2.7.7.7;

Protein crystallography data

The structure of Post-Catalytic Complex of Human Polymerase Mu (G433A) Mutant with Incoming Dttp, PDB code: 5vz9 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) 35.15 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.190, 68.847, 111.355, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 19.1

Other elements in 5vz9:

The structure of Post-Catalytic Complex of Human Polymerase Mu (G433A) 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 (G433A) Mutant with Incoming Dttp (pdb code 5vz9). 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 (G433A) Mutant with Incoming Dttp, PDB code: 5vz9:

Chlorine binding site 1 out of 1 in 5vz9

Go back to Chlorine Binding Sites List in 5vz9
Chlorine binding site 1 out of 1 in the Post-Catalytic Complex of Human Polymerase Mu (G433A) 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 (G433A) Mutant with Incoming Dttp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:11.8
occ:0.70
 N A:SER458 3.2 7.5 1.0
OG A:SER458 3.2 11.0 1.0
O1 A:EDO506 3.3 24.1 1.0
CB A:SER458 3.5 9.9 1.0
O4' T:DA7 3.5 18.6 1.0
NH1 A:ARG445 3.6 10.4 1.0
NH2 A:ARG445 3.6 7.1 1.0
C1' T:DA7 3.6 16.4 1.0
C4' T:DA7 3.6 20.9 1.0
CB A:ASN457 3.7 8.2 1.0
O2 T:DT6 3.9 10.1 1.0
CZ A:ARG445 3.9 7.0 1.0
CA A:SER458 3.9 7.2 1.0
CA A:ASN457 4.1 7.3 1.0
C A:ASN457 4.1 9.2 1.0
O2 A:EDO506 4.2 14.8 1.0
C2' T:DA7 4.3 17.6 1.0
NH2 A:ARG387 4.4 16.7 1.0
C1 A:EDO506 4.4 29.2 1.0
C1' T:DT6 4.5 13.0 1.0
C5' T:DA7 4.5 32.0 1.0
CG A:ASN457 4.6 11.7 1.0
C3' T:DA7 4.6 17.9 1.0
N9 T:DA7 4.7 13.5 1.0
O3' T:DT6 4.8 13.1 1.0
C2 T:DT6 4.9 9.5 1.0
C2 A:EDO506 5.0 23.3 1.0
C A:SER458 5.0 7.8 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: Sat Jul 12 10:04:47 2025

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