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Zinc in PDB 4pi2: Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc

Enzymatic activity of Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc

All present enzymatic activity of Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc:
1.14.18.3;

Protein crystallography data

The structure of Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc, PDB code: 4pi2 was solved by S.Sirajuddin, A.C.Rosenzweig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 3.33
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 120.857, 185.450, 192.777, 90.00, 90.00, 90.00
R / Rfree (%) 22.5 / 28.2

Other elements in 4pi2:

The structure of Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc also contains other interesting chemical elements:

Arsenic (As) 1 atom
Copper (Cu) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc (pdb code 4pi2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc, PDB code: 4pi2:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in 4pi2

Go back to Zinc Binding Sites List in 4pi2
Zinc binding site 1 out of 5 in the Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Zn301

b:64.3
occ:1.00
 OE2 G:GLU201 1.6 53.5 1.0
OD2 G:ASP129 1.9 35.6 1.0
NE2 G:HIS146 2.1 44.1 1.0
NE2 G:HIS133 2.2 65.1 1.0
CD G:GLU201 2.6 51.2 1.0
CG G:ASP129 2.8 35.2 1.0
CE1 G:HIS133 2.8 66.2 1.0
CE1 G:HIS146 2.9 43.8 1.0
OD1 G:ASP129 3.0 34.1 1.0
OE1 G:GLU201 3.1 49.2 1.0
CD2 G:HIS146 3.1 41.8 1.0
CD2 G:HIS133 3.4 64.3 1.0
CG G:GLU201 3.8 51.5 1.0
ND1 G:HIS133 4.0 65.8 1.0
ND1 G:HIS146 4.1 41.2 1.0
CB G:ASP129 4.2 34.1 1.0
CG G:HIS146 4.2 40.1 1.0
CG G:HIS133 4.3 59.9 1.0
OE2 G:GLU149 4.4 30.8 1.0
CE2 G:PHE150 4.8 31.1 1.0
CB G:GLU201 5.0 53.9 1.0
CZ G:PHE150 5.0 30.2 1.0

Zinc binding site 2 out of 5 in 4pi2

Go back to Zinc Binding Sites List in 4pi2
Zinc binding site 2 out of 5 in the Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Zn302

b:0.8
occ:1.00
 OD2 G:ASP93 2.5 74.5 1.0
ND1 G:HIS177 2.9 71.3 1.0
CE1 G:HIS177 3.1 72.4 1.0
CG G:ASP93 3.2 66.7 1.0
OD1 G:ASP93 3.4 62.7 1.0
CG G:HIS177 4.2 70.6 1.0
NE2 G:HIS177 4.4 72.5 1.0
CB G:ASP93 4.5 62.5 1.0
CD2 G:HIS177 4.9 72.5 1.0
CB G:HIS177 5.0 67.0 1.0

Zinc binding site 3 out of 5 in 4pi2

Go back to Zinc Binding Sites List in 4pi2
Zinc binding site 3 out of 5 in the Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
K:Zn301

b:67.3
occ:1.00
 OD2 K:ASP129 1.8 37.8 1.0
NE2 K:HIS146 1.9 55.5 1.0
NE2 K:HIS133 2.2 62.1 1.0
OE2 K:GLU201 2.2 48.5 1.0
CG K:ASP129 2.6 37.0 1.0
OD1 K:ASP129 2.6 37.2 1.0
CE1 K:HIS133 2.7 65.6 1.0
CD2 K:HIS146 2.9 55.5 1.0
CD K:GLU201 2.9 52.1 1.0
CE1 K:HIS146 2.9 54.4 1.0
OE1 K:GLU201 3.1 52.0 1.0
CD2 K:HIS133 3.3 57.5 1.0
ND1 K:HIS133 3.9 61.1 1.0
ND1 K:HIS146 4.0 57.7 1.0
CG K:HIS146 4.0 57.0 1.0
CB K:ASP129 4.0 37.8 1.0
CG K:GLU201 4.1 55.5 1.0
CG K:HIS133 4.2 58.0 1.0
O K:ASP129 4.6 39.0 1.0
OE2 K:GLU149 4.7 38.7 1.0

Zinc binding site 4 out of 5 in 4pi2

Go back to Zinc Binding Sites List in 4pi2
Zinc binding site 4 out of 5 in the Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn301

b:66.4
occ:1.00
 OE2 C:GLU201 1.7 71.6 1.0
OD2 C:ASP129 1.9 53.4 1.0
NE2 C:HIS146 2.0 53.1 1.0
NE2 C:HIS133 2.2 60.0 1.0
CD C:GLU201 2.5 71.1 1.0
CG C:ASP129 2.8 52.8 1.0
CE1 C:HIS133 2.8 58.9 1.0
CE1 C:HIS146 2.9 52.9 1.0
OE1 C:GLU201 2.9 68.5 1.0
OD1 C:ASP129 3.0 52.8 1.0
CD2 C:HIS146 3.1 52.5 1.0
CD2 C:HIS133 3.3 59.4 1.0
CG C:GLU201 3.8 68.4 1.0
ND1 C:HIS133 4.0 61.3 1.0
ND1 C:HIS146 4.0 53.5 1.0
CG C:HIS146 4.2 52.5 1.0
CB C:ASP129 4.2 53.7 1.0
CG C:HIS133 4.3 61.9 1.0
OE2 C:GLU149 4.5 51.4 1.0
CE2 C:PHE150 4.9 54.0 1.0
O C:ASP129 4.9 43.7 1.0
CB C:GLU201 5.0 70.0 1.0
CZ C:PHE150 5.0 50.4 1.0

Zinc binding site 5 out of 5 in 4pi2

Go back to Zinc Binding Sites List in 4pi2
Zinc binding site 5 out of 5 in the Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Particulate Methane Monooxygenase From Methylocystis Sp. Atcc 49242 (Rockwell) Soaked in Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn302

b:0.1
occ:1.00
 O2 C:CAC303 2.2 0.1 1.0
OD2 C:ASP93 2.3 64.8 1.0
ND1 C:HIS177 2.3 71.2 1.0
CE1 C:HIS177 2.4 68.0 1.0
OD1 C:ASP93 2.7 58.9 1.0
CG C:ASP93 2.8 62.8 1.0
AS C:CAC303 3.5 0.3 1.0
O1 C:CAC303 3.6 95.9 1.0
CG C:HIS177 3.7 70.1 1.0
NE2 C:HIS177 3.7 65.7 1.0
CB C:ASP93 4.3 67.5 1.0
CD2 C:HIS177 4.3 67.8 1.0
CB C:HIS177 4.6 70.5 1.0
C2 C:CAC303 4.6 92.1 1.0
CG1 C:VAL92 4.9 68.8 1.0
C1 C:CAC303 4.9 95.7 1.0

Reference:

S.Sirajuddin, D.Barupala, S.Helling, K.Marcus, T.L.Stemmler, A.C.Rosenzweig. Effects of Zinc on Particulate Methane Monooxygenase Activity and Structure. J.Biol.Chem. V. 289 21782 2014.
ISSN: ESSN 1083-351X
PubMed: 24942740
DOI: 10.1074/JBC.M114.581363
Page generated: Sun Oct 27 05:54:25 2024

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