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Magnesium in PDB 1xsn: Crystal Structure of Human Dna Polymerase Lambda in Complex with A One Nucleotide Dna Gap and Ddttp

Enzymatic activity of Crystal Structure of Human Dna Polymerase Lambda in Complex with A One Nucleotide Dna Gap and Ddttp

All present enzymatic activity of Crystal Structure of Human Dna Polymerase Lambda in Complex with A One Nucleotide Dna Gap and Ddttp:
2.7.7.7;

Protein crystallography data

The structure of Crystal Structure of Human Dna Polymerase Lambda in Complex with A One Nucleotide Dna Gap and Ddttp, PDB code: 1xsn was solved by M.Garcia-Diaz, K.Bebenek, J.M.Krahn, T.A.Kunkel, L.C.Pedersen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.84 / 1.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.043, 62.551, 139.830, 90.00, 90.00, 90.00
R / Rfree (%) 21.3 / 25.5

Other elements in 1xsn:

The structure of Crystal Structure of Human Dna Polymerase Lambda in Complex with A One Nucleotide Dna Gap and Ddttp also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Dna Polymerase Lambda in Complex with A One Nucleotide Dna Gap and Ddttp (pdb code 1xsn). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Human Dna Polymerase Lambda in Complex with A One Nucleotide Dna Gap and Ddttp, PDB code: 1xsn:

Magnesium binding site 1 out of 1 in 1xsn

Go back to Magnesium Binding Sites List in 1xsn
Magnesium binding site 1 out of 1 in the Crystal Structure of Human Dna Polymerase Lambda in Complex with A One Nucleotide Dna Gap and Ddttp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human Dna Polymerase Lambda in Complex with A One Nucleotide Dna Gap and Ddttp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg576

b:30.9
occ:1.00
 O1B A:D3T579 1.9 30.8 1.0
O1A A:D3T579 2.0 26.7 1.0
OD2 A:ASP427 2.0 28.6 1.0
OD2 A:ASP429 2.1 28.3 1.0
O A:HOH586 2.2 35.5 1.0
O3G A:D3T579 2.2 29.8 1.0
PB A:D3T579 3.0 31.4 1.0
CG A:ASP427 3.1 30.1 1.0
CG A:ASP429 3.1 29.4 1.0
PA A:D3T579 3.2 30.4 1.0
PG A:D3T579 3.4 32.8 1.0
O3A A:D3T579 3.4 29.5 1.0
OD1 A:ASP429 3.4 26.9 1.0
O3B A:D3T579 3.5 31.5 1.0
OD1 A:ASP427 3.6 31.7 1.0
O A:HOH636 3.7 36.0 1.0
O1G A:D3T579 3.9 32.2 1.0
O A:ASP427 3.9 27.9 1.0
C5' A:D3T579 4.1 30.7 1.0
O5' A:D3T579 4.1 29.6 1.0
N A:ASP427 4.2 27.5 1.0
OG A:SER417 4.2 28.9 1.0
C A:ASP427 4.2 28.3 1.0
CB A:ASP427 4.3 28.4 1.0
O2A A:D3T579 4.3 29.6 1.0
O2B A:D3T579 4.4 29.9 1.0
O A:HOH589 4.4 27.2 1.0
N A:SER417 4.4 31.9 1.0
CB A:ASP429 4.5 28.5 1.0
O2G A:D3T579 4.5 30.9 1.0
CA A:ASP427 4.5 28.4 1.0
CA A:GLY416 4.6 32.2 1.0
N A:ASP429 4.8 30.1 1.0
N A:VAL428 4.9 29.3 1.0
CB A:SER417 5.0 31.3 1.0

Reference:

M.Garcia-Diaz, K.Bebenek, J.M.Krahn, T.A.Kunkel, L.C.Pedersen. A Closed Conformation For the Pol Lambda Catalytic Cycle. Nat.Struct.Mol.Biol. V. 12 97 2005.
ISSN: ISSN 1545-9993
PubMed: 15608652
DOI: 10.1038/NSMB876
Page generated: Tue Aug 13 18:23:14 2024

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