Atomistry » Copper » PDB 3qjq-3t6v » 3rgb
Atomistry »
  Copper »
    PDB 3qjq-3t6v »
      3rgb »

Copper in PDB 3rgb: Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath)

Enzymatic activity of Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath)

All present enzymatic activity of Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath):
1.14.13.25;

Protein crystallography data

The structure of Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath), PDB code: 3rgb was solved by S.M.Smith, A.C.Rosenzweig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.46 / 2.80
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 264.140, 264.140, 150.010, 90.00, 90.00, 90.00
R / Rfree (%) 26.9 / 29.6

Other elements in 3rgb:

The structure of Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath) also contains other interesting chemical elements:

Zinc (Zn) 9 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath) (pdb code 3rgb). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 9 binding sites of Copper where determined in the Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath), PDB code: 3rgb:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9;

Copper binding site 1 out of 9 in 3rgb

Go back to Copper Binding Sites List in 3rgb
Copper binding site 1 out of 9 in the Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu415

b:58.9
occ:1.00
 ND1 A:HIS48 2.0 45.6 1.0
ND1 A:HIS72 2.0 41.1 1.0
CE1 A:HIS48 2.8 46.1 1.0
CG A:HIS48 2.8 44.3 1.0
OE1 A:GLN404 2.9 57.6 1.0
CG A:HIS72 3.0 39.9 1.0
CE1 A:HIS72 3.0 42.7 1.0
CB A:HIS48 3.3 42.2 1.0
CB A:HIS72 3.3 38.1 1.0
CD A:GLN404 3.8 58.5 1.0
NE2 A:HIS48 3.8 47.2 1.0
O A:HIS72 3.9 38.0 1.0
CD2 A:HIS48 3.9 46.5 1.0
CD2 A:LEU390 4.0 39.4 1.0
NE2 A:HIS72 4.1 44.2 1.0
CD2 A:HIS72 4.1 42.3 1.0
C A:HIS72 4.2 38.1 1.0
CA A:PHE74 4.2 41.3 1.0
NE2 A:GLN404 4.3 60.7 1.0
N A:HIS48 4.3 41.8 1.0
CA A:HIS72 4.3 38.1 1.0
CB A:PHE74 4.4 40.7 1.0
CA A:HIS48 4.4 42.0 1.0
N A:PHE74 4.4 40.6 1.0
CD2 A:PHE74 4.5 41.9 1.0
CG A:LEU390 4.6 39.8 1.0
C A:VAL73 4.8 40.0 1.0
CD1 A:LEU390 4.8 39.5 1.0
CG A:GLN404 4.9 54.4 1.0
CG A:PHE74 5.0 41.4 1.0

Copper binding site 2 out of 9 in 3rgb

Go back to Copper Binding Sites List in 3rgb
Copper binding site 2 out of 9 in the Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu416

b:91.5
occ:1.00
 CU1 A:CUA416 0.0 91.5 1.0
ND1 A:HIS33 2.4 55.7 1.0
CU2 A:CUA416 2.7 76.3 1.0
CG A:HIS33 2.9 56.9 1.0
NE2 A:HIS139 3.0 43.9 1.0
N A:HIS33 3.1 56.8 1.0
O A:HIS137 3.1 48.8 1.0
CD2 A:HIS139 3.2 44.8 1.0
CB A:HIS33 3.2 57.1 1.0
CE1 A:HIS33 3.2 58.2 1.0
CB A:HIS137 3.5 50.5 1.0
CA A:HIS33 3.7 57.0 1.0
CD2 A:HIS33 3.9 57.7 1.0
NE2 A:HIS33 4.0 59.1 1.0
C A:HIS137 4.1 48.7 1.0
CG A:HIS137 4.1 53.1 1.0
CE1 A:HIS139 4.3 45.8 1.0
CA A:HIS137 4.4 50.1 1.0
ND1 A:HIS137 4.5 57.4 1.0
O A:GLY92 4.5 48.1 1.0
CG A:HIS139 4.5 44.0 1.0
O A:HIS33 4.6 55.8 1.0
C A:HIS33 4.7 56.6 1.0
N A:HIS137 4.9 50.8 1.0
CD A:PRO94 5.0 49.5 1.0

Copper binding site 3 out of 9 in 3rgb

Go back to Copper Binding Sites List in 3rgb
Copper binding site 3 out of 9 in the Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu416

b:76.3
occ:1.00
 CU2 A:CUA416 0.0 76.3 1.0
ND1 A:HIS33 2.2 55.7 1.0
NE2 A:HIS139 2.3 43.9 1.0
ND1 A:HIS137 2.6 57.4 1.0
CU1 A:CUA416 2.7 91.5 1.0
N A:HIS33 2.7 56.8 1.0
CE1 A:HIS33 2.7 58.2 1.0
CG A:HIS137 2.8 53.1 1.0
CE1 A:HIS139 3.0 45.8 1.0
CE1 A:HIS137 3.1 57.4 1.0
CB A:HIS137 3.3 50.5 1.0
CD2 A:HIS139 3.4 44.8 1.0
CG A:HIS33 3.5 56.9 1.0
CD2 A:HIS137 3.5 55.1 1.0
NE2 A:HIS137 3.6 56.2 1.0
CA A:HIS33 3.9 57.0 1.0
NE2 A:HIS33 4.0 59.1 1.0
CB A:HIS33 4.1 57.1 1.0
ND1 A:HIS139 4.2 43.9 1.0
O A:HIS137 4.2 48.8 1.0
CD2 A:HIS33 4.4 57.7 1.0
CG A:HIS139 4.4 44.0 1.0
CA A:HIS137 4.6 50.1 1.0
C A:HIS137 4.6 48.7 1.0
CA A:GLY154 4.6 48.7 1.0
OE1 A:GLU35 4.7 60.9 1.0
OE2 A:GLU35 4.8 60.8 1.0

Copper binding site 4 out of 9 in 3rgb

Go back to Copper Binding Sites List in 3rgb
Copper binding site 4 out of 9 in the Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cu415

b:58.5
occ:1.00
 ND1 E:HIS72 1.8 37.5 1.0
ND1 E:HIS48 2.0 42.8 1.0
CE1 E:HIS48 2.7 43.8 1.0
CG E:HIS72 2.8 37.1 1.0
CE1 E:HIS72 2.8 39.4 1.0
OE1 E:GLN404 3.0 55.3 1.0
CG E:HIS48 3.1 42.0 1.0
CB E:HIS72 3.2 35.7 1.0
CD E:GLN404 3.7 55.2 1.0
CB E:HIS48 3.7 40.3 1.0
NE2 E:HIS48 3.8 45.8 1.0
CD2 E:LEU390 3.8 35.8 1.0
O E:HIS72 3.9 35.3 1.0
NE2 E:HIS72 3.9 40.8 1.0
CD2 E:HIS72 4.0 38.9 1.0
CD2 E:HIS48 4.1 44.0 1.0
NE2 E:GLN404 4.1 58.0 1.0
CA E:PHE74 4.2 39.2 1.0
C E:HIS72 4.2 35.8 1.0
CA E:HIS72 4.3 35.7 1.0
CB E:PHE74 4.5 38.8 1.0
N E:PHE74 4.5 38.5 1.0
CD2 E:PHE74 4.5 40.0 1.0
N E:HIS48 4.6 39.8 1.0
CG E:GLN404 4.7 51.1 1.0
CG E:LEU390 4.7 36.8 1.0
C E:VAL73 4.7 37.7 1.0
O E:VAL73 4.8 37.3 1.0
CA E:HIS48 4.8 40.0 1.0
CG E:PHE74 4.9 39.7 1.0
CB E:GLN404 5.0 48.8 1.0
OE1 E:GLU75 5.0 51.7 1.0

Copper binding site 5 out of 9 in 3rgb

Go back to Copper Binding Sites List in 3rgb
Copper binding site 5 out of 9 in the Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cu416

b:59.2
occ:1.00
 CU1 E:CUA416 0.0 59.2 1.0
ND1 E:HIS33 1.7 57.8 1.0
NE2 E:HIS139 2.3 44.9 1.0
N E:HIS33 2.4 58.7 1.0
CE1 E:HIS33 2.6 60.0 1.0
CG E:HIS33 2.6 59.8 1.0
CU2 E:CUA416 2.7 79.2 1.0
CD2 E:HIS139 3.0 45.6 1.0
CB E:HIS33 3.2 59.7 1.0
CA E:HIS33 3.3 59.1 1.0
CE1 E:HIS139 3.4 46.1 1.0
CB E:HIS137 3.5 52.0 1.0
NE2 E:HIS33 3.6 62.4 1.0
CG E:HIS137 3.6 54.5 1.0
CD2 E:HIS33 3.6 61.2 1.0
ND1 E:HIS137 3.7 58.4 1.0
O E:HIS137 3.8 49.8 1.0
CG E:HIS139 4.3 44.7 1.0
ND1 E:HIS139 4.4 44.1 1.0
C E:HIS33 4.4 58.2 1.0
CD2 E:HIS137 4.4 56.6 1.0
CE1 E:HIS137 4.5 59.3 1.0
C E:HIS137 4.5 50.0 1.0
O E:HIS33 4.6 57.5 1.0
CA E:HIS137 4.6 51.8 1.0
OE2 E:GLU35 4.7 62.2 1.0
NE2 E:HIS137 4.9 57.8 1.0

Copper binding site 6 out of 9 in 3rgb

Go back to Copper Binding Sites List in 3rgb
Copper binding site 6 out of 9 in the Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cu416

b:79.2
occ:1.00
 CU2 E:CUA416 0.0 79.2 1.0
ND1 E:HIS137 2.4 58.4 1.0
NE2 E:HIS139 2.4 44.9 1.0
CE1 E:HIS137 2.5 59.3 1.0
CG E:HIS137 2.5 54.5 1.0
NE2 E:HIS137 2.6 57.8 1.0
CU1 E:CUA416 2.7 59.2 1.0
CD2 E:HIS137 2.7 56.6 1.0
CE1 E:HIS139 2.9 46.1 1.0
CD2 E:HIS139 3.4 45.6 1.0
ND1 E:HIS33 3.4 57.8 1.0
CA E:GLY154 3.5 48.7 1.0
CB E:HIS137 3.5 52.0 1.0
CE1 E:HIS33 3.7 60.0 1.0
N E:HIS33 3.8 58.7 1.0
ND1 E:HIS139 3.9 44.1 1.0
C E:GLY154 4.0 49.9 1.0
O E:GLY154 4.2 50.7 1.0
N E:GLY154 4.2 47.3 1.0
CG E:HIS139 4.2 44.7 1.0
OE1 E:GLU35 4.2 61.5 1.0
CA E:HIS137 4.6 51.8 1.0
O E:HIS137 4.6 49.8 1.0
C E:HIS137 4.7 50.0 1.0
OH E:TYR374 4.7 59.5 1.0
CG E:HIS33 4.8 59.8 1.0
N E:LYS155 4.9 50.0 1.0
NE2 E:HIS33 5.0 62.4 1.0

Copper binding site 7 out of 9 in 3rgb

Go back to Copper Binding Sites List in 3rgb
Copper binding site 7 out of 9 in the Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Cu415

b:51.5
occ:1.00
 ND1 I:HIS72 1.9 45.8 1.0
ND1 I:HIS48 2.1 51.1 1.0
CE1 I:HIS48 2.8 51.9 1.0
CG I:HIS72 2.9 44.8 1.0
CE1 I:HIS72 2.9 47.0 1.0
OE1 I:GLN404 3.0 63.6 1.0
CG I:HIS48 3.1 50.2 1.0
CB I:HIS72 3.2 43.4 1.0
CB I:HIS48 3.6 48.6 1.0
CD I:GLN404 3.8 64.1 1.0
NE2 I:HIS48 3.9 53.3 1.0
CD2 I:LEU390 3.9 46.0 1.0
O I:HIS72 3.9 42.3 1.0
NE2 I:HIS72 4.0 48.1 1.0
CD2 I:HIS72 4.0 46.3 1.0
CD2 I:HIS48 4.0 52.3 1.0
CA I:PHE74 4.1 45.4 1.0
NE2 I:GLN404 4.2 66.3 1.0
C I:HIS72 4.2 42.6 1.0
CB I:PHE74 4.3 45.1 1.0
CA I:HIS72 4.3 42.8 1.0
N I:PHE74 4.4 44.3 1.0
CD2 I:PHE74 4.4 46.6 1.0
N I:HIS48 4.5 47.1 1.0
C I:VAL73 4.7 43.5 1.0
CA I:HIS48 4.7 47.8 1.0
CG I:LEU390 4.8 47.0 1.0
O I:VAL73 4.9 43.3 1.0
CG I:PHE74 4.9 45.9 1.0
CG I:GLN404 4.9 60.6 1.0

Copper binding site 8 out of 9 in 3rgb

Go back to Copper Binding Sites List in 3rgb
Copper binding site 8 out of 9 in the Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Cu416

b:85.4
occ:1.00
 CU1 I:CUA416 0.0 85.4 1.0
N I:HIS33 1.9 63.4 1.0
NE2 I:HIS139 2.2 50.5 1.0
ND1 I:HIS33 2.4 62.5 1.0
CU2 I:CUA416 2.7 74.5 1.0
CD2 I:HIS139 2.7 51.0 1.0
CB I:HIS33 2.8 63.5 1.0
CA I:HIS33 2.8 63.2 1.0
CG I:HIS33 2.9 63.7 1.0
CE1 I:HIS139 3.4 52.0 1.0
CE1 I:HIS33 3.5 64.8 1.0
C I:HIS33 3.7 62.2 1.0
O I:HIS33 3.8 61.3 1.0
CG I:HIS139 3.9 50.0 1.0
O I:HIS137 4.0 54.9 1.0
CD2 I:HIS33 4.1 64.7 1.0
ND1 I:HIS139 4.2 50.0 1.0
CB I:HIS137 4.3 57.6 1.0
OE2 I:GLU35 4.4 67.2 1.0
NE2 I:HIS33 4.4 66.2 1.0
CG I:HIS137 4.5 60.8 1.0
ND1 I:HIS137 4.6 64.5 1.0
C I:HIS137 4.9 55.3 1.0
N I:GLY34 4.9 62.2 1.0

Copper binding site 9 out of 9 in 3rgb

Go back to Copper Binding Sites List in 3rgb
Copper binding site 9 out of 9 in the Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 9 of Crystal Structure of Particulate Methane Monooxygenase From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Cu416

b:74.5
occ:1.00
 CU2 I:CUA416 0.0 74.5 1.0
ND1 I:HIS137 2.3 64.5 1.0
NE2 I:HIS139 2.3 50.5 1.0
CG I:HIS137 2.4 60.8 1.0
ND1 I:HIS33 2.6 62.5 1.0
CU1 I:CUA416 2.7 85.4 1.0
CE1 I:HIS137 2.7 65.4 1.0
CE1 I:HIS33 3.0 64.8 1.0
CD2 I:HIS137 3.0 63.1 1.0
CE1 I:HIS139 3.1 52.0 1.0
CB I:HIS137 3.1 57.6 1.0
NE2 I:HIS137 3.1 64.4 1.0
N I:HIS33 3.3 63.4 1.0
CD2 I:HIS139 3.4 51.0 1.0
CG I:HIS33 4.0 63.7 1.0
ND1 I:HIS139 4.2 50.0 1.0
O I:HIS137 4.2 54.9 1.0
CA I:GLY154 4.3 55.8 1.0
NE2 I:HIS33 4.3 66.2 1.0
CA I:HIS137 4.3 57.1 1.0
CG I:HIS139 4.4 50.0 1.0
C I:HIS137 4.4 55.3 1.0
CA I:HIS33 4.5 63.2 1.0
OE1 I:GLU35 4.6 67.5 1.0
CB I:HIS33 4.7 63.5 1.0
CD2 I:HIS33 4.8 64.7 1.0
C I:GLY154 4.8 57.1 1.0
N I:GLY154 5.0 55.1 1.0
OE2 I:GLU35 5.0 67.2 1.0
O I:GLY154 5.0 58.4 1.0

Reference:

S.M.Smith, S.Rawat, J.Telser, B.M.Hoffman, T.L.Stemmler, A.C.Rosenzweig. Crystal Structure and Characterization of Particulate Methane Monooxygenase From Methylocystis Species Strain M. Biochemistry V. 50 10231 2011.
ISSN: ISSN 0006-2960
PubMed: 22013879
DOI: 10.1021/BI200801Z
Page generated: Wed Jul 31 01:39:30 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy