Atomistry » Manganese » PDB 1g15-1hkd » 1g15
Atomistry »
  Manganese »
    PDB 1g15-1hkd »
      1g15 »

Manganese in PDB 1g15: Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site

Enzymatic activity of Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site

All present enzymatic activity of Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site:
3.1.26.4;

Protein crystallography data

The structure of Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site, PDB code: 1g15 was solved by E.R.Goedken, S.Marqusee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 71.653, 71.653, 48.127, 90.00, 90.00, 120.00
R / Rfree (%) 22.3 / 26.1

Manganese Binding Sites:

The binding sites of Manganese atom in the Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site (pdb code 1g15). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site, PDB code: 1g15:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1g15

Go back to Manganese Binding Sites List in 1g15
Manganese binding site 1 out of 2 in the Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn201

b:17.0
occ:1.00
O A:HOH239 2.1 17.3 1.0
OE2 A:GLU48 2.1 21.8 1.0
OD2 A:ASP10 2.2 14.1 1.0
O A:HOH204 2.2 13.7 1.0
OD1 A:ASP70 2.3 15.5 1.0
O A:HOH203 2.9 16.1 1.0
CD A:GLU48 3.2 20.6 1.0
CG A:ASP70 3.3 17.6 1.0
CG A:ASP10 3.3 12.4 1.0
OD2 A:ASP70 3.5 19.1 1.0
OE1 A:GLU48 3.6 21.8 1.0
OD1 A:ASP10 3.7 12.4 1.0
MN A:MN202 4.0 12.7 1.0
O A:GLY11 4.2 16.1 1.0
O A:HOH241 4.2 10.2 1.0
N A:GLY11 4.3 13.2 1.0
O A:HOH247 4.4 42.6 1.0
N A:SER71 4.4 13.9 1.0
ND2 A:ASN44 4.5 22.4 1.0
OD1 A:ASN44 4.5 24.6 1.0
C A:ASP70 4.5 14.1 1.0
CG A:GLU48 4.5 19.2 1.0
CB A:ASP10 4.5 14.3 1.0
CA A:SER71 4.6 17.3 1.0
CA A:ASP10 4.7 13.0 1.0
CB A:ASP70 4.7 16.8 1.0
O A:HOH243 4.7 37.1 1.0
O A:ASP70 4.7 14.0 1.0
O A:HOH242 4.8 21.7 1.0
CB A:SER71 4.8 16.9 1.0
O A:HOH240 4.9 16.5 1.0
CG A:ASN44 5.0 19.5 1.0

Manganese binding site 2 out of 2 in 1g15

Go back to Manganese Binding Sites List in 1g15
Manganese binding site 2 out of 2 in the Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Co-Crystal of E. Coli Rnase Hi with Two MN2+ Ions Bound in the the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn202

b:12.7
occ:1.00
OD1 A:ASP134 2.1 12.6 1.0
O A:HOH240 2.2 16.5 1.0
O A:HOH241 2.2 10.2 1.0
OD1 A:ASP10 2.2 12.4 1.0
O A:HOH204 2.4 13.7 1.0
CG A:ASP134 3.2 12.0 1.0
CG A:ASP10 3.2 12.4 1.0
OD2 A:ASP10 3.5 14.1 1.0
CB A:ASP134 3.8 12.3 1.0
O A:HOH239 3.9 17.3 1.0
MN A:MN201 4.0 17.0 1.0
OD2 A:ASP70 4.1 19.1 1.0
O A:GLY11 4.2 16.1 1.0
OD2 A:ASP134 4.2 13.4 1.0
O A:HOH219 4.2 24.3 1.0
CA A:ASP134 4.3 13.6 1.0
NE A:ARG138 4.3 11.2 1.0
NH2 A:ARG138 4.4 10.2 1.0
CB A:ASP10 4.6 14.3 1.0
CZ A:ARG138 4.8 13.8 1.0
O A:HOH220 4.9 36.1 1.0
OD1 A:ASP70 4.9 15.5 1.0
CG A:ASP70 4.9 17.6 1.0

Reference:

E.R.Goedken, S.Marqusee. Co-Crystal of Escherichia Coli Rnase Hi with MN2+ Ions Reveals Two Divalent Metals Bound in the Active Site. J.Biol.Chem. V. 276 7266 2001.
ISSN: ISSN 0021-9258
PubMed: 11083878
DOI: 10.1074/JBC.M009626200
Page generated: Sat Oct 5 10:31:31 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