Atomistry » Arsenic » PDB 7jry-8cff » 7kg1
Atomistry »
  Arsenic »
    PDB 7jry-8cff »
      7kg1 »

Arsenic in PDB 7kg1: Structure of Human Parg Complexed with Parg-002

Enzymatic activity of Structure of Human Parg Complexed with Parg-002

All present enzymatic activity of Structure of Human Parg Complexed with Parg-002:
3.2.1.143;

Protein crystallography data

The structure of Structure of Human Parg Complexed with Parg-002, PDB code: 7kg1 was solved by C.A.Brosey, L.P.F.Balapiti-Modarage, L.S.Warden, D.E.Jones, Z.Ahmed, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.66 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 66.463, 88.964, 95.049, 90, 90, 90
R / Rfree (%) 17.4 / 19.8

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Structure of Human Parg Complexed with Parg-002 (pdb code 7kg1). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Structure of Human Parg Complexed with Parg-002, PDB code: 7kg1:

Arsenic binding site 1 out of 1 in 7kg1

Go back to Arsenic Binding Sites List in 7kg1
Arsenic binding site 1 out of 1 in the Structure of Human Parg Complexed with Parg-002


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Structure of Human Parg Complexed with Parg-002 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As1008

b:62.1
occ:1.00
AS A:CAC1008 0.0 62.1 1.0
O2 A:CAC1008 1.7 48.5 1.0
O1 A:CAC1008 1.7 51.6 1.0
C2 A:CAC1008 2.0 56.4 1.0
C1 A:CAC1008 2.0 55.1 1.0
H A:ARG644 2.9 43.7 1.0
HH12 A:ARG535 2.9 66.8 1.0
HH22 A:ARG535 3.2 70.9 1.0
HD21 A:ASN646 3.2 44.4 1.0
HH A:TYR564 3.3 55.8 1.0
HH11 A:ARG644 3.5 52.4 1.0
O A:HOH1101 3.6 45.5 1.0
NH1 A:ARG535 3.6 55.6 1.0
HE2 A:TYR564 3.7 49.3 1.0
N A:ARG644 3.7 36.4 1.0
O A:HOH1117 3.7 38.4 1.0
HA A:ARG644 3.7 46.8 1.0
NH2 A:ARG535 3.9 59.0 1.0
HB2 A:ASN646 4.0 42.0 1.0
HA A:PRO643 4.0 39.0 1.0
ND2 A:ASN646 4.0 36.9 1.0
OH A:TYR564 4.1 46.5 1.0
HD3 A:ARG644 4.1 52.8 1.0
NH1 A:ARG644 4.1 43.6 1.0
CZ A:ARG535 4.2 55.9 1.0
HH12 A:ARG644 4.2 52.4 1.0
HH11 A:ARG535 4.2 66.8 1.0
CA A:ARG644 4.3 38.9 1.0
HD22 A:ASN646 4.4 44.4 1.0
CE2 A:TYR564 4.5 41.0 1.0
HH21 A:ARG535 4.5 70.9 1.0
H A:ARG645 4.6 40.3 1.0
H A:ASN646 4.7 44.1 1.0
CA A:PRO643 4.7 32.4 1.0
C A:PRO643 4.7 34.1 1.0
CZ A:TYR564 4.8 43.8 1.0
CB A:ASN646 4.9 34.9 1.0
HB2 A:PRO643 4.9 40.9 1.0
CG A:ASN646 5.0 34.7 1.0
O A:HOH1385 5.0 44.7 1.0

Reference:

C.A.Brosey, J.H.Houl, P.Katsonis, L.P.F.Balapiti-Modarage, S.Bommagani, A.Arvai, D.Moiani, A.Bacolla, T.Link, L.S.Warden, O.Lichtarge, D.E.Jones, Z.Ahmed, J.A.Tainer. Targeting Sars-Cov-2 NSP3 Macrodomain Structure with Insights From Human Poly(Adp-Ribose) Glycohydrolase (Parg) Structures with Inhibitors. Prog.Biophys.Mol.Biol. 2021.
ISSN: ISSN 0079-6107
PubMed: 33636189
DOI: 10.1016/J.PBIOMOLBIO.2021.02.002
Page generated: Wed Jul 10 13:49:20 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy