Atomistry » Manganese » PDB 1xif-1ytm » 1yd4
Atomistry »
  Manganese »
    PDB 1xif-1ytm »
      1yd4 »

Manganese in PDB 1yd4: Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Thermotoga Maritima: Point Mutant Y29F Bound to Its Catalytic Divalent Cation

Protein crystallography data

The structure of Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Thermotoga Maritima: Point Mutant Y29F Bound to Its Catalytic Divalent Cation, PDB code: 1yd4 was solved by J.J.Truglio, B.Rhau, D.L.Croteau, L.Wang, M.Skorvaga, E.Karakas, M.J.Dellavecchia, H.Wang, B.Van Houten, C.Kisker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.90
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 54.949, 54.949, 109.187, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 20.6

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Thermotoga Maritima: Point Mutant Y29F Bound to Its Catalytic Divalent Cation (pdb code 1yd4). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Thermotoga Maritima: Point Mutant Y29F Bound to Its Catalytic Divalent Cation, PDB code: 1yd4:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in 1yd4

Go back to Manganese Binding Sites List in 1yd4
Manganese binding site 1 out of 3 in the Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Thermotoga Maritima: Point Mutant Y29F Bound to Its Catalytic Divalent Cation


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Thermotoga Maritima: Point Mutant Y29F Bound to Its Catalytic Divalent Cation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1001

b:35.9
occ:1.00
OE2 A:GLU76 2.1 22.2 1.0
O A:HOH1034 2.1 31.1 1.0
O A:HOH1123 2.1 22.4 1.0
O A:HOH1022 2.3 24.1 1.0
O A:HOH1059 2.3 41.7 1.0
O A:HOH1058 2.3 37.1 1.0
CD A:GLU76 3.0 21.4 1.0
OE1 A:GLU76 3.4 25.9 1.0
O A:HOH1073 3.7 49.5 1.0
O A:HOH1031 4.1 30.5 1.0
O A:HOH1082 4.2 52.6 1.0
CA A:GLY31 4.3 16.4 1.0
O A:HOH1115 4.3 65.6 1.0
O A:ILE30 4.4 16.6 1.0
CG A:GLU76 4.4 17.3 1.0
N A:LYS32 4.5 18.5 1.0
O A:HOH1025 4.6 26.9 1.0
CD1 A:ILE80 4.7 21.3 1.0
CG A:LYS32 4.8 22.2 1.0
C A:GLY31 4.9 17.0 1.0

Manganese binding site 2 out of 3 in 1yd4

Go back to Manganese Binding Sites List in 1yd4
Manganese binding site 2 out of 3 in the Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Thermotoga Maritima: Point Mutant Y29F Bound to Its Catalytic Divalent Cation


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Thermotoga Maritima: Point Mutant Y29F Bound to Its Catalytic Divalent Cation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1002

b:52.5
occ:1.00
O A:HOH1043 3.2 44.6 1.0
CB A:ASN68 3.6 22.1 1.0
CG A:ASN68 3.6 23.3 1.0
CG A:ARG70 3.7 22.4 1.0
ND2 A:ASN68 3.7 21.2 1.0
CD A:ARG70 3.8 23.6 1.0
OD1 A:ASN68 4.0 18.9 1.0
N A:ARG70 4.5 19.4 1.0
CB A:ARG70 4.5 20.3 1.0
N A:GLU69 4.6 20.8 1.0
O A:HOH1102 4.8 67.6 1.0
CA A:ASN68 4.9 20.8 1.0

Manganese binding site 3 out of 3 in 1yd4

Go back to Manganese Binding Sites List in 1yd4
Manganese binding site 3 out of 3 in the Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Thermotoga Maritima: Point Mutant Y29F Bound to Its Catalytic Divalent Cation


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Thermotoga Maritima: Point Mutant Y29F Bound to Its Catalytic Divalent Cation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1004

b:67.8
occ:1.00
OE1 A:GLU60 2.2 35.5 1.0
OE2 A:GLU62 2.3 40.4 1.0
O A:HOH1074 2.6 49.6 1.0
CD A:GLU60 3.1 29.6 1.0
CD A:GLU62 3.3 32.2 1.0
OE2 A:GLU60 3.4 31.6 1.0
NZ A:LYS22 3.7 34.6 1.0
CG A:GLU62 3.7 30.6 1.0
OE1 A:GLU62 4.4 34.0 1.0
CG A:GLU60 4.4 26.9 1.0
CE A:LYS22 4.5 30.8 1.0
CD A:LYS22 4.5 26.0 1.0

Reference:

J.J.Truglio, B.Rhau, D.L.Croteau, L.Wang, M.Skorvaga, E.Karakas, M.J.Dellavecchia, H.Wang, B.Van Houten, C.Kisker. Structural Insights Into the First Incision Reaction During Nucleotide Excision Repair Embo J. V. 24 885 2005.
ISSN: ISSN 0261-4189
PubMed: 15692561
DOI: 10.1038/SJ.EMBOJ.7600568
Page generated: Sat Oct 5 13:11:47 2024

Last articles

F in 5ALN
F in 5ALJ
F in 5ALC
F in 5ALB
F in 5AKH
F in 5AJR
F in 5AIX
F in 5AKE
F in 5AK2
F in 5AFK
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy