Atomistry » Iron » PDB 1mpy-1n5u » 1mty
Atomistry »
  Iron »
    PDB 1mpy-1n5u »
      1mty »

Iron in PDB 1mty: Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath)

Enzymatic activity of Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath)

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

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath), PDB code: 1mty was solved by A.C.Rosenzweig, P.Nordlund, S.J.Lippard, C.A.Frederick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.700, 109.600, 330.200, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath) (pdb code 1mty). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath), PDB code: 1mty:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1mty

Go back to Iron Binding Sites List in 1mty
Iron binding site 1 out of 4 in the Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe3

b:22.3
occ:1.00
 O D:HOH639 1.9 11.8 1.0
OE2 D:GLU243 2.0 19.0 1.0
OE2 D:GLU209 2.0 16.7 1.0
ND1 D:HIS246 2.2 12.3 1.0
H2 D:HOH639 2.4 0.0 1.0
H1 D:HOH639 2.4 0.0 1.0
OE2 D:GLU144 2.4 9.7 1.0
O D:HOH641 2.6 18.0 1.0
H2 D:HOH641 2.7 0.0 1.0
CD D:GLU209 2.9 17.8 1.0
CE1 D:HIS246 3.0 12.6 1.0
CD D:GLU243 3.0 25.5 1.0
FE D:FE4 3.0 8.5 1.0
HE22 D:GLN140 3.2 0.0 1.0
CD D:GLU144 3.3 9.8 1.0
CG D:HIS246 3.4 13.4 1.0
H2 D:HOH640 3.4 0.0 1.0
OE1 D:GLU243 3.4 26.5 1.0
OE1 D:GLU144 3.5 10.1 1.0
H1 D:HOH641 3.5 0.0 1.0
CG D:GLU209 3.7 15.6 1.0
NE2 D:GLN140 3.7 9.9 1.0
O D:HOH640 3.8 25.8 1.0
OE1 D:GLU209 3.8 15.0 1.0
HE21 D:GLN140 3.9 0.0 1.0
CB D:HIS246 3.9 14.2 1.0
H1 D:HOH640 4.0 0.0 1.0
NE2 D:HIS246 4.2 11.6 1.0
CG D:GLU243 4.4 24.0 1.0
CD2 D:HIS246 4.4 13.3 1.0
ND1 D:HIS147 4.5 6.3 1.0
CE1 D:HIS147 4.5 5.8 1.0
CD D:GLN140 4.6 10.8 1.0
OE1 D:GLU114 4.6 12.1 1.0
CG D:GLU144 4.8 6.7 1.0
CB D:GLU209 4.8 17.2 1.0
CG D:GLN140 4.9 11.1 1.0

Iron binding site 2 out of 4 in 1mty

Go back to Iron Binding Sites List in 1mty
Iron binding site 2 out of 4 in the Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe4

b:8.5
occ:1.00
 H1 D:HOH639 0.9 0.0 1.0
O D:HOH639 1.8 11.8 1.0
H1 D:HOH640 1.8 0.0 1.0
H2 D:HOH639 1.9 0.0 1.0
OE1 D:GLU114 1.9 12.1 1.0
OE1 D:GLU144 2.0 10.1 1.0
H2 D:HOH640 2.1 0.0 1.0
ND1 D:HIS147 2.1 6.3 1.0
O D:HOH640 2.3 25.8 1.0
O D:HOH641 2.4 18.0 1.0
H1 D:HOH641 2.7 0.0 1.0
CD D:GLU114 3.0 12.2 1.0
CD D:GLU144 3.0 9.8 1.0
CE1 D:HIS147 3.0 5.8 1.0
FE D:FE3 3.0 22.3 1.0
CG D:HIS147 3.2 6.4 1.0
OE2 D:GLU144 3.3 9.7 1.0
H2 D:HOH641 3.3 0.0 1.0
OE2 D:GLU114 3.4 13.2 1.0
CB D:HIS147 3.6 8.3 1.0
OE1 D:GLU243 3.9 26.5 1.0
OE2 D:GLU243 4.1 19.0 1.0
NE2 D:HIS147 4.2 6.7 1.0
CG D:GLU114 4.3 11.0 1.0
CE1 D:HIS246 4.3 12.6 1.0
CD2 D:HIS147 4.3 8.2 1.0
CG D:GLU144 4.4 6.7 1.0
ND1 D:HIS246 4.5 12.3 1.0
CD D:GLU243 4.5 25.5 1.0
OE2 D:GLU209 4.5 16.7 1.0
CB D:GLU114 4.6 7.9 1.0
CA D:GLU144 4.6 6.6 1.0
CG2 D:ILE239 4.6 7.3 1.0
CA D:GLU114 4.7 6.8 1.0
H1 D:HOH642 4.7 0.0 1.0
CB D:GLU144 4.8 6.8 1.0

Iron binding site 3 out of 4 in 1mty

Go back to Iron Binding Sites List in 1mty
Iron binding site 3 out of 4 in the Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe1

b:21.2
occ:1.00
 H1 E:HOH584 1.4 0.0 1.0
OE2 E:GLU209 1.8 19.5 1.0
H2 E:HOH584 2.0 0.0 1.0
O E:HOH584 2.0 18.4 1.0
OE2 E:GLU243 2.0 23.5 1.0
ND1 E:HIS246 2.1 13.2 1.0
O E:HOH586 2.5 15.2 1.0
OE2 E:GLU144 2.6 11.8 1.0
H1 E:HOH586 2.8 0.0 1.0
CE1 E:HIS246 2.9 9.6 1.0
CD E:GLU209 3.0 21.1 1.0
CD E:GLU243 3.0 27.0 1.0
FE E:FE2 3.1 11.6 1.0
HE22 E:GLN140 3.1 0.0 1.0
H2 E:HOH586 3.2 0.0 1.0
CG E:HIS246 3.2 12.3 1.0
OE1 E:GLU243 3.3 31.4 1.0
H1 E:HOH585 3.4 0.0 1.0
CD E:GLU144 3.5 10.5 1.0
NE2 E:GLN140 3.6 9.1 1.0
OE1 E:GLU144 3.7 12.4 1.0
CB E:HIS246 3.7 13.3 1.0
CG E:GLU209 3.8 18.0 1.0
HE21 E:GLN140 3.8 0.0 1.0
OE1 E:GLU209 3.8 19.3 1.0
H2 E:HOH585 4.0 0.0 1.0
O E:HOH585 4.1 10.3 1.0
NE2 E:HIS246 4.1 15.0 1.0
CD2 E:HIS246 4.3 13.7 1.0
CG E:GLU243 4.4 24.2 1.0
CD E:GLN140 4.5 9.5 1.0
ND1 E:HIS147 4.5 5.7 1.0
CE1 E:HIS147 4.6 6.4 1.0
CB E:GLU209 4.8 18.9 1.0
OE1 E:GLU114 4.9 13.5 1.0
CG E:GLN140 4.9 9.7 1.0
CG E:GLU144 4.9 7.7 1.0
HE2 E:HIS246 4.9 0.0 1.0

Iron binding site 4 out of 4 in 1mty

Go back to Iron Binding Sites List in 1mty
Iron binding site 4 out of 4 in the Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe2

b:11.6
occ:1.00
 H2 E:HOH584 1.2 0.0 1.0
H1 E:HOH585 1.5 0.0 1.0
O E:HOH584 1.6 18.4 1.0
OE1 E:GLU114 2.0 13.5 1.0
ND1 E:HIS147 2.2 5.7 1.0
OE1 E:GLU144 2.2 12.4 1.0
O E:HOH586 2.2 15.2 1.0
H2 E:HOH585 2.2 0.0 1.0
O E:HOH585 2.3 10.3 1.0
H1 E:HOH584 2.3 0.0 1.0
H1 E:HOH586 2.9 0.0 1.0
H2 E:HOH586 2.9 0.0 1.0
CD E:GLU114 3.0 15.0 1.0
CE1 E:HIS147 3.1 6.4 1.0
CD E:GLU144 3.1 10.5 1.0
FE E:FE1 3.1 21.2 1.0
CG E:HIS147 3.2 5.4 1.0
OE2 E:GLU144 3.4 11.8 1.0
OE2 E:GLU114 3.5 19.8 1.0
CB E:HIS147 3.6 5.7 1.0
OE1 E:GLU243 3.9 31.4 1.0
NE2 E:HIS147 4.3 7.4 1.0
CE1 E:HIS246 4.3 9.6 1.0
CD2 E:HIS147 4.3 6.9 1.0
CG E:GLU114 4.4 11.7 1.0
OE2 E:GLU243 4.4 23.5 1.0
ND1 E:HIS246 4.4 13.2 1.0
CG E:GLU144 4.5 7.7 1.0
OE2 E:GLU209 4.6 19.5 1.0
CD E:GLU243 4.6 27.0 1.0
CB E:GLU114 4.7 10.6 1.0
CG2 E:ILE239 4.7 10.7 1.0
CA E:GLU114 4.7 8.3 1.0
CA E:GLU144 4.7 6.8 1.0
CB E:GLU144 5.0 5.8 1.0

Reference:

A.C.Rosenzweig, H.Brandstetter, D.A.Whittington, P.Nordlund, S.J.Lippard, C.A.Frederick. Crystal Structures of the Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath): Implications For Substrate Gating and Component Interactions. Proteins V. 29 141 1997.
ISSN: ISSN 0887-3585
PubMed: 9329079
DOI: 10.1002/(SICI)1097-0134(199710)29:2<141::AID-PROT2>3.3.CO;2-W
Page generated: Sat Aug 3 11:07:35 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy