Atomistry » Magnesium » PDB 1u3g-1uet » 1u6k
Atomistry »
  Magnesium »
    PDB 1u3g-1uet »
      1u6k »

Magnesium in PDB 1u6k: Tls Refinement of the Structure of Se-Methionine Labelled Coenzyme F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase (Mtd) From Methanopyrus Kandleri

Enzymatic activity of Tls Refinement of the Structure of Se-Methionine Labelled Coenzyme F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase (Mtd) From Methanopyrus Kandleri

All present enzymatic activity of Tls Refinement of the Structure of Se-Methionine Labelled Coenzyme F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase (Mtd) From Methanopyrus Kandleri:
1.5.99.9;

Protein crystallography data

The structure of Tls Refinement of the Structure of Se-Methionine Labelled Coenzyme F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase (Mtd) From Methanopyrus Kandleri, PDB code: 1u6k was solved by E.Warkentin, C.H.Hagemeier, S.Shima, R.K.Thauer, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.55
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 120.100, 151.200, 110.000, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 19.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Tls Refinement of the Structure of Se-Methionine Labelled Coenzyme F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase (Mtd) From Methanopyrus Kandleri (pdb code 1u6k). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Tls Refinement of the Structure of Se-Methionine Labelled Coenzyme F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase (Mtd) From Methanopyrus Kandleri, PDB code: 1u6k:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1u6k

Go back to Magnesium Binding Sites List in 1u6k
Magnesium binding site 1 out of 4 in the Tls Refinement of the Structure of Se-Methionine Labelled Coenzyme F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase (Mtd) From Methanopyrus Kandleri


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Tls Refinement of the Structure of Se-Methionine Labelled Coenzyme F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase (Mtd) From Methanopyrus Kandleri within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg5001

b:19.2
occ:1.00
O A:HOH4034 1.9 22.2 1.0
O A:HOH4014 1.9 22.0 1.0
O A:HOH4009 2.1 18.9 1.0
OE1 A:GLU175 3.9 26.1 1.0
O A:HOH4004 4.2 17.1 1.0
O A:GLU91 4.3 24.8 1.0
O A:HOH4030 4.3 20.4 1.0
O A:SER90 4.4 26.1 1.0
O A:HOH4124 4.5 26.8 1.0
C A:GLU91 4.6 24.9 1.0
CG A:GLU175 4.7 25.2 1.0
CD A:GLU175 4.7 26.0 1.0
N A:PRO93 4.9 21.4 1.0
CA A:GLU91 4.9 26.9 1.0
CA A:PRO93 5.0 21.2 1.0
O A:HOH4036 5.0 21.9 1.0
O A:HOH4077 5.0 26.4 1.0
C A:TYR92 5.0 21.7 1.0

Magnesium binding site 2 out of 4 in 1u6k

Go back to Magnesium Binding Sites List in 1u6k
Magnesium binding site 2 out of 4 in the Tls Refinement of the Structure of Se-Methionine Labelled Coenzyme F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase (Mtd) From Methanopyrus Kandleri


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Tls Refinement of the Structure of Se-Methionine Labelled Coenzyme F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase (Mtd) From Methanopyrus Kandleri within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg5002

b:23.5
occ:1.00
O A:HOH4036 1.9 21.9 1.0
O A:HOH4190 2.0 29.0 1.0
O A:HOH4488 2.0 27.1 1.0
O A:HOH4089 2.2 28.5 1.0
O A:GLU111 4.1 27.3 1.0
OE1 A:GLU175 4.2 26.1 1.0
O A:HOH4124 4.3 26.8 1.0
OE2 A:GLU175 4.4 29.1 1.0
O A:HOH4204 4.4 29.7 1.0
O A:HOH4491 4.6 38.2 1.0
CD A:GLU175 4.7 26.0 1.0
C A:GLN112 5.0 24.2 1.0

Magnesium binding site 3 out of 4 in 1u6k

Go back to Magnesium Binding Sites List in 1u6k
Magnesium binding site 3 out of 4 in the Tls Refinement of the Structure of Se-Methionine Labelled Coenzyme F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase (Mtd) From Methanopyrus Kandleri


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Tls Refinement of the Structure of Se-Methionine Labelled Coenzyme F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase (Mtd) From Methanopyrus Kandleri within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg5003

b:30.3
occ:1.00
O A:HOH4091 2.0 29.9 1.0
O A:HOH4213 2.0 34.8 1.0
O A:HOH4510 2.1 30.9 1.0
O A:HOH4210 2.2 31.0 1.0
OE1 A:GLU91 4.1 42.1 1.0
O A:HOH4346 4.2 33.6 1.0
O A:GLU91 4.4 24.8 1.0
O A:HOH4092 4.4 26.9 1.0
O A:HOH4570 4.4 41.7 1.0
OD2 A:ASP171 4.6 36.1 1.0
O A:HOH4302 4.9 38.5 1.0

Magnesium binding site 4 out of 4 in 1u6k

Go back to Magnesium Binding Sites List in 1u6k
Magnesium binding site 4 out of 4 in the Tls Refinement of the Structure of Se-Methionine Labelled Coenzyme F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase (Mtd) From Methanopyrus Kandleri


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Tls Refinement of the Structure of Se-Methionine Labelled Coenzyme F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase (Mtd) From Methanopyrus Kandleri within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg5004

b:37.2
occ:1.00
O A:HOH4180 2.0 32.2 1.0
O A:HOH4178 2.1 34.7 1.0
O A:HOH4279 2.1 34.0 1.0
O A:HOH4361 2.2 33.8 1.0
O A:HOH4471 3.9 35.1 1.0
OD1 A:ASP177 4.0 31.4 1.0
OD2 A:ASP177 4.2 29.9 1.0
O A:GLU172 4.2 33.5 1.0
O A:HOH4409 4.3 40.7 1.0
OE2 A:GLU172 4.4 42.3 1.0
CG A:ASP177 4.5 27.9 1.0
CB A:GLU172 4.6 35.9 1.0

Reference:

E.Warkentin, C.H.Hagemeier, S.Shima, R.K.Thauer, U.Ermler. The Structure of F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase: A Crystallographic 'Superstructure' of the Selenomethionine-Labelled Protein Crystal Structure. Acta Crystallogr.,Sect.D V. 61 198 2005.
ISSN: ISSN 0907-4449
PubMed: 15681872
DOI: 10.1107/S0907444904030732
Page generated: Mon Dec 14 06:52:37 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy