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Potassium in PDB 2i2x: Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri

Enzymatic activity of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri

All present enzymatic activity of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri:
2.1.1.90;

Protein crystallography data

The structure of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri, PDB code: 2i2x was solved by C.H.Hagemeier, M.Kruer, R.K.Thauer, E.Warkentin, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 101.750, 172.850, 190.540, 90.00, 98.86, 90.00
R / Rfree (%) 18.2 / 23.1

Other elements in 2i2x:

The structure of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri also contains other interesting chemical elements:

Cobalt (Co) 8 atoms
Zinc (Zn) 12 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri (pdb code 2i2x). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 8 binding sites of Potassium where determined in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri, PDB code: 2i2x:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Potassium binding site 1 out of 8 in 2i2x

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Potassium binding site 1 out of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K511

b:23.5
occ:0.70
OE2 A:GLU86 2.3 19.5 1.0
OE2 A:GLU164 2.4 24.6 1.0
ZN A:ZN501 2.9 20.9 1.0
OE1 A:GLU313 3.2 13.9 1.0
CD A:GLU86 3.2 17.9 1.0
CD A:GLU164 3.2 20.5 1.0
OE1 A:GLU86 3.4 20.6 1.0
OE1 A:GLU164 3.4 22.3 1.0
O A:HOH609 3.6 8.4 1.0
NZ A:LYS267 4.0 14.7 1.0
CD A:GLU313 4.1 14.7 1.0
SG A:CYS269 4.3 14.2 1.0
OE2 A:GLU313 4.3 13.8 1.0
CG A:GLU164 4.6 15.3 1.0
CG A:GLU86 4.6 15.6 1.0
CE A:LYS267 4.7 14.4 1.0
SG A:CYS220 4.9 14.5 1.0
O B:HOH501 4.9 42.7 1.0

Potassium binding site 2 out of 8 in 2i2x

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Potassium binding site 2 out of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K512

b:22.0
occ:0.70
OE2 C:GLU86 2.3 22.1 1.0
OE2 C:GLU164 2.5 17.9 1.0
O C:HOH679 2.8 13.8 1.0
ZN C:ZN502 3.0 19.9 1.0
OE1 C:GLU313 3.1 15.3 1.0
CD C:GLU86 3.1 19.0 1.0
OE1 C:GLU86 3.3 21.1 1.0
CD C:GLU164 3.3 15.8 1.0
OE1 C:GLU164 3.5 18.0 1.0
O C:HOH518 3.9 9.5 1.0
CD C:GLU313 4.0 13.5 1.0
NZ C:LYS267 4.1 9.2 1.0
OE2 C:GLU313 4.2 16.9 1.0
SG C:CYS269 4.4 14.3 1.0
CG C:GLU86 4.5 14.6 1.0
O D:HOH501 4.6 20.5 1.0
CG C:GLU164 4.7 13.6 1.0
CE C:LYS267 4.9 10.7 1.0
SG C:CYS220 5.0 10.5 1.0

Potassium binding site 3 out of 8 in 2i2x

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Potassium binding site 3 out of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe atom residue distance (Å) B Occ
E:K513

b:33.9
occ:0.70
OE2 E:GLU86 2.5 42.1 1.0
OE2 E:GLU164 2.6 38.4 1.0
OE1 E:GLU313 2.9 37.9 1.0
ZN E:ZN503 3.0 37.0 0.7
CD E:GLU86 3.2 41.7 1.0
OE1 E:GLU86 3.3 41.2 1.0
CD E:GLU164 3.5 36.3 1.0
OE1 E:GLU164 3.6 38.0 1.0
CD E:GLU313 3.8 37.1 1.0
OE2 E:GLU313 4.0 38.0 1.0
NZ E:LYS267 4.3 26.5 1.0
SG E:CYS269 4.4 36.4 1.0
CG E:GLU86 4.7 38.2 1.0
O E:GLU313 4.7 32.8 1.0
O F:HOH501 4.9 17.7 0.5
CG E:GLU164 5.0 34.0 1.0

Potassium binding site 4 out of 8 in 2i2x

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Potassium binding site 4 out of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe atom residue distance (Å) B Occ
G:K514

b:40.0
occ:0.70
OE2 G:GLU86 2.5 33.7 1.0
OE2 G:GLU164 2.5 34.1 1.0
ZN G:ZN504 3.0 33.2 0.7
OE1 G:GLU313 3.2 30.7 1.0
CD G:GLU164 3.2 33.3 1.0
OE1 G:GLU164 3.2 34.5 1.0
CD G:GLU86 3.4 33.6 1.0
OE1 G:GLU86 3.7 33.6 1.0
O H:HOH501 4.0 18.1 0.5
CD G:GLU313 4.2 30.3 1.0
O G:HOH555 4.3 20.5 1.0
NZ G:LYS267 4.4 29.1 1.0
SG G:CYS269 4.5 28.3 1.0
OE2 G:GLU313 4.5 32.8 1.0
SG G:CYS220 4.6 28.3 1.0
CG G:GLU164 4.6 32.3 1.0
CG G:GLU86 4.7 32.2 1.0
O39 H:B13500 4.9 61.4 1.0

Potassium binding site 5 out of 8 in 2i2x

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Potassium binding site 5 out of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe atom residue distance (Å) B Occ
I:K515

b:28.7
occ:0.70
OE2 I:GLU164 2.4 25.7 1.0
OE2 I:GLU86 2.6 29.5 1.0
ZN I:ZN505 3.0 30.0 1.0
OE1 I:GLU313 3.1 23.1 1.0
CD I:GLU164 3.3 25.1 1.0
CD I:GLU86 3.4 28.8 1.0
OE1 I:GLU86 3.4 30.6 1.0
OE1 I:GLU164 3.5 28.1 1.0
CD I:GLU313 3.9 20.6 1.0
OE2 I:GLU313 3.9 22.1 1.0
O I:HOH525 4.1 13.2 1.0
NZ I:LYS267 4.2 21.3 1.0
SG I:CYS269 4.4 18.5 1.0
O J:HOH501 4.4 2.8 0.5
CG I:GLU164 4.7 22.1 1.0
CG I:GLU86 4.7 23.4 1.0
SG I:CYS220 5.0 21.9 1.0
CE I:LYS267 5.0 20.9 1.0

Potassium binding site 6 out of 8 in 2i2x

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Potassium binding site 6 out of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 6 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe atom residue distance (Å) B Occ
K:K516

b:31.9
occ:0.70
OE2 K:GLU164 2.4 30.9 1.0
OE2 K:GLU86 2.6 27.5 1.0
OE1 K:GLU313 2.9 20.8 1.0
ZN K:ZN506 3.0 33.5 1.0
CD K:GLU164 3.2 29.8 1.0
OE1 K:GLU164 3.3 33.9 1.0
CD K:GLU86 3.4 26.6 1.0
OE1 K:GLU86 3.6 28.3 1.0
CD K:GLU313 3.9 18.8 1.0
O K:HOH605 3.9 19.9 1.0
NZ K:LYS267 4.0 20.8 1.0
OE2 K:GLU313 4.1 19.6 1.0
SG K:CYS269 4.5 24.8 1.0
CG K:GLU86 4.5 25.2 1.0
CG K:GLU164 4.6 25.1 1.0
SG K:CYS220 4.9 24.5 1.0
CE K:LYS267 4.9 20.1 1.0
O L:HOH501 5.0 18.9 0.5

Potassium binding site 7 out of 8 in 2i2x

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Potassium binding site 7 out of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 7 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe atom residue distance (Å) B Occ
M:K517

b:33.7
occ:0.70
OE2 M:GLU164 2.3 29.0 1.0
OE2 M:GLU86 2.4 34.6 1.0
O M:HOH615 2.6 27.2 1.0
ZN M:ZN507 3.0 33.9 1.0
OE1 M:GLU313 3.1 22.9 1.0
CD M:GLU164 3.2 28.2 1.0
OE1 M:GLU164 3.3 32.0 1.0
CD M:GLU86 3.4 31.7 1.0
OE1 M:GLU86 3.8 33.7 1.0
NZ M:LYS267 4.0 14.2 1.0
CD M:GLU313 4.0 21.6 1.0
O M:HOH563 4.3 12.4 1.0
OE2 M:GLU313 4.3 23.2 1.0
SG M:CYS269 4.4 22.7 1.0
O N:HOH501 4.5 10.9 0.5
CG M:GLU164 4.6 24.6 1.0
CG M:GLU86 4.7 27.5 1.0
CE M:LYS267 5.0 14.6 1.0

Potassium binding site 8 out of 8 in 2i2x

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Potassium binding site 8 out of 8 in the Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 8 of Crystal Structure of Methanol:Cobalamin Methyltransferase Complex Mtabc From Methanosarcina Barkeri within 5.0Å range:
probe atom residue distance (Å) B Occ
O:K518

b:35.2
occ:0.70
OE2 O:GLU86 2.3 26.5 1.0
OE2 O:GLU164 2.5 27.9 1.0
ZN O:ZN508 3.0 33.9 1.0
OE1 O:GLU313 3.1 25.0 1.0
CD O:GLU86 3.2 25.4 1.0
CD O:GLU164 3.3 27.0 1.0
OE1 O:GLU164 3.4 30.5 1.0
OE1 O:GLU86 3.5 27.0 1.0
CD O:GLU313 3.9 23.7 1.0
O O:HOH577 4.0 6.5 1.0
O P:HOH501 4.0 2.0 0.5
OE2 O:GLU313 4.1 25.7 1.0
NZ O:LYS267 4.2 17.6 1.0
CG O:GLU86 4.5 20.5 1.0
SG O:CYS269 4.6 19.2 1.0
SG O:CYS220 4.8 21.4 1.0
CG O:GLU164 4.8 23.2 1.0

Reference:

C.H.Hagemeier, M.Krer, R.K.Thauer, E.Warkentin, U.Ermler. Insight Into the Mechanism of Biological Methanol Activation Based on the Crystal Structure of the Methanol-Cobalamin Methyltransferase Complex Proc.Natl.Acad.Sci.Usa V. 103 18917 2006.
ISSN: ISSN 0027-8424
PubMed: 17142327
DOI: 10.1073/PNAS.0603650103
Page generated: Mon Aug 12 06:38:48 2024

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