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Manganese in PDB 1yd5: Crystal Structure of the Giy-Yig N-Terminal Endonuclease Domain of Uvrc From Thermotoga Maritima: Point Mutant N88A 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 N88A Bound to Its Catalytic Divalent Cation, PDB code: 1yd5 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 / 1.80
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 55.315, 55.315, 108.711, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 20.9

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 N88A Bound to Its Catalytic Divalent Cation (pdb code 1yd5). 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 N88A Bound to Its Catalytic Divalent Cation, PDB code: 1yd5:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in 1yd5

Go back to Manganese Binding Sites List in 1yd5
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 N88A 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 N88A Bound to Its Catalytic Divalent Cation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1001

b:25.4
occ:1.00
OE2 A:GLU76 2.1 22.7 1.0
O A:HOH1086 2.2 30.6 1.0
O A:HOH1079 2.2 25.2 1.0
O A:HOH1084 2.2 19.5 1.0
O A:HOH1069 2.2 35.4 1.0
O A:HOH1085 2.2 30.3 1.0
CD A:GLU76 3.1 23.4 1.0
OE1 A:GLU76 3.5 28.2 1.0
O A:HOH1026 4.0 28.6 1.0
O A:HOH1022 4.1 32.0 1.0
CA A:GLY31 4.2 19.3 1.0
OH A:TYR29 4.3 26.8 1.0
O A:ILE30 4.3 19.4 1.0
CG A:GLU76 4.4 19.1 1.0
N A:LYS32 4.4 21.1 1.0
O A:HOH1011 4.7 25.8 1.0
CD1 A:ILE80 4.7 21.9 1.0
CG A:LYS32 4.8 23.5 1.0
C A:GLY31 4.9 20.1 1.0

Manganese binding site 2 out of 3 in 1yd5

Go back to Manganese Binding Sites List in 1yd5
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 N88A 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 N88A Bound to Its Catalytic Divalent Cation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1002

b:39.8
occ:1.00
O A:HOH1050 3.1 45.5 1.0
CG A:ASN68 3.6 19.5 1.0
CB A:ASN68 3.6 20.0 1.0
CG A:ARG70 3.7 21.4 1.0
CD A:ARG70 3.9 21.8 1.0
OD1 A:ASN68 3.9 19.5 1.0
ND2 A:ASN68 4.0 21.1 1.0
N A:ARG70 4.4 19.5 1.0
CB A:ARG70 4.5 20.5 1.0
N A:GLU69 4.5 21.5 1.0
O A:HOH1080 4.8 44.2 1.0
CA A:ASN68 4.9 20.0 1.0
C A:ASN68 5.0 21.0 1.0

Manganese binding site 3 out of 3 in 1yd5

Go back to Manganese Binding Sites List in 1yd5
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 N88A 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 N88A Bound to Its Catalytic Divalent Cation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1004

b:62.3
occ:1.00
OE1 A:GLU60 2.1 33.5 1.0
CD A:GLU60 3.2 28.1 1.0
OE2 A:GLU60 3.6 30.4 1.0
O A:HOH1076 3.9 64.2 1.0
NZ A:LYS22 4.0 33.1 1.0
CG A:GLU60 4.4 25.7 1.0
OE1 A:GLU62 4.6 35.8 1.0
CE A:LYS22 4.7 29.1 1.0
CD A:LYS22 4.7 24.4 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 13:12:07 2024

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