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Calcium in PDB 4rno: Crystal Structure of Human Polymerase Eta Extending An Abasic Site-Da Pair By Inserting Dctp Opposite Template G

Enzymatic activity of Crystal Structure of Human Polymerase Eta Extending An Abasic Site-Da Pair By Inserting Dctp Opposite Template G

All present enzymatic activity of Crystal Structure of Human Polymerase Eta Extending An Abasic Site-Da Pair By Inserting Dctp Opposite Template G:
2.7.7.7;

Protein crystallography data

The structure of Crystal Structure of Human Polymerase Eta Extending An Abasic Site-Da Pair By Inserting Dctp Opposite Template G, PDB code: 4rno was solved by A.Patra, M.Egli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.78 / 2.82
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 98.788, 98.788, 82.008, 90.00, 90.00, 120.00
R / Rfree (%) 24.1 / 28.2

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Human Polymerase Eta Extending An Abasic Site-Da Pair By Inserting Dctp Opposite Template G (pdb code 4rno). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Human Polymerase Eta Extending An Abasic Site-Da Pair By Inserting Dctp Opposite Template G, PDB code: 4rno:

Calcium binding site 1 out of 1 in 4rno

Go back to Calcium Binding Sites List in 4rno
Calcium binding site 1 out of 1 in the Crystal Structure of Human Polymerase Eta Extending An Abasic Site-Da Pair By Inserting Dctp Opposite Template G


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Human Polymerase Eta Extending An Abasic Site-Da Pair By Inserting Dctp Opposite Template G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca502

b:47.2
occ:1.00
 O1B A:DCP501 2.2 48.8 1.0
OD1 A:ASP13 2.3 47.3 1.0
O2A A:DCP501 2.4 49.1 1.0
O1G A:DCP501 2.4 48.5 1.0
OD1 A:ASP115 2.4 48.1 1.0
OD2 A:ASP13 2.4 47.8 1.0
O3A A:DCP501 2.5 49.2 1.0
O A:MET14 2.5 47.9 1.0
PB A:DCP501 2.7 48.0 1.0
CG A:ASP13 2.7 47.3 1.0
PA A:DCP501 2.9 48.5 1.0
O3B A:DCP501 3.2 48.9 1.0
PG A:DCP501 3.3 47.9 1.0
CG A:ASP115 3.6 48.0 1.0
O5' A:DCP501 3.6 50.5 1.0
C5' A:DCP501 3.6 49.8 1.0
C A:MET14 3.7 47.4 1.0
O A:HOH646 4.0 49.2 1.0
O2G A:DCP501 4.1 49.7 1.0
O2B A:DCP501 4.1 49.6 1.0
OD2 A:ASP115 4.1 48.8 1.0
N A:MET14 4.2 47.1 1.0
O1A A:DCP501 4.2 50.1 1.0
CB A:ASP13 4.2 47.8 1.0
N A:CYS16 4.5 48.6 1.0
CA A:MET14 4.5 46.9 1.0
O3G A:DCP501 4.6 49.0 1.0
NZ A:LYS231 4.6 49.5 1.0
N A:PHE17 4.6 48.3 1.0
N A:ASP15 4.7 48.3 1.0
C A:ASP13 4.7 47.1 1.0
C4' A:DCP501 4.7 49.4 1.0
CA A:ASP15 4.8 48.8 1.0
CB A:ASP115 4.8 48.2 1.0
CB A:PHE17 4.8 47.6 1.0
O3' A:DCP501 4.9 49.1 1.0
C A:ASP15 5.0 48.5 1.0
CA A:ASP13 5.0 47.5 1.0

Reference:

A.Patra, Q.Zhang, L.Lei, Y.Su, M.Egli, F.P.Guengerich. Structural and Kinetic Analysis of Nucleoside Triphosphate Incorporation Opposite An Abasic Site By Human Translesion Dna Polymerase Eta J.Biol.Chem. 2015.
ISSN: ESSN 1083-351X
DOI: 10.1074/JBC.M115.637561
Page generated: Sun Jul 14 12:44:54 2024

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