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Iron in PDB 1mmo: Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane

Enzymatic activity of Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane

All present enzymatic activity of Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane:
1.14.13.25;

Protein crystallography data

The structure of Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane, PDB code: 1mmo was solved by A.C.Rosenzweig, C.A.Frederick, S.J.Lippard, P.Nordlund, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 62.600, 110.100, 333.500, 90.00, 90.00, 90.00
R / Rfree (%) 17 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane (pdb code 1mmo). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane, PDB code: 1mmo:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1mmo

Go back to Iron Binding Sites List in 1mmo
Iron binding site 1 out of 4 in the Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe3

b:18.7
occ:1.00
 HD1 D:HIS246 1.2 0.0 1.0
H1 D:HOH621 1.7 0.0 1.0
OE2 D:GLU243 1.8 19.4 1.0
O D:HOH621 2.0 16.8 1.0
ND1 D:HIS246 2.2 17.9 1.0
O D:ACY1 2.3 37.2 1.0
OE2 D:GLU209 2.4 21.3 1.0
OE2 D:GLU144 2.6 6.6 1.0
H2 D:HOH621 2.6 0.0 1.0
CD D:GLU243 2.8 22.7 1.0
CE1 D:HIS246 3.0 16.7 1.0
CD D:GLU209 3.2 17.3 1.0
OE1 D:GLU243 3.2 28.6 1.0
CG D:HIS246 3.2 17.9 1.0
C D:ACY1 3.3 36.5 1.0
FE D:FE4 3.5 11.3 1.0
CD D:GLU144 3.5 6.2 1.0
HE22 D:GLN140 3.5 0.0 1.0
OE1 D:GLU144 3.6 8.9 1.0
OXT D:ACY1 3.6 38.7 1.0
CG D:GLU209 3.6 17.7 1.0
CB D:HIS246 3.8 15.7 1.0
NE2 D:GLN140 3.9 10.6 1.0
HD1 D:HIS147 4.0 0.0 1.0
OE1 D:GLU209 4.1 17.8 1.0
CG D:GLU243 4.2 22.1 1.0
HE21 D:GLN140 4.2 0.0 1.0
NE2 D:HIS246 4.2 20.8 1.0
H1 D:HOH620 4.2 0.0 1.0
O D:HOH620 4.3 20.8 1.0
CD2 D:HIS246 4.4 16.2 1.0
H2 D:HOH620 4.5 0.0 1.0
CH3 D:ACY1 4.6 38.5 1.0
CB D:GLU209 4.7 14.2 1.0
CD D:GLN140 4.7 14.2 1.0
ND1 D:HIS147 4.7 7.9 1.0
CG D:GLU144 4.9 2.0 1.0
CE1 D:HIS147 4.9 6.4 1.0
CG D:GLN140 5.0 12.8 1.0

Iron binding site 2 out of 4 in 1mmo

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Iron binding site 2 out of 4 in the Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe4

b:11.3
occ:1.00
 HD1 D:HIS147 1.3 0.0 1.0
H2 D:HOH621 1.6 0.0 1.0
O D:HOH621 1.7 16.8 1.0
H1 D:HOH621 1.8 0.0 1.0
OE1 D:GLU114 1.9 8.7 1.0
H1 D:HOH620 2.0 0.0 1.0
OE1 D:GLU144 2.1 8.9 1.0
O D:HOH620 2.2 20.8 1.0
ND1 D:HIS147 2.3 7.9 1.0
OXT D:ACY1 2.6 38.7 1.0
CD D:GLU114 2.9 13.6 1.0
H2 D:HOH620 3.1 0.0 1.0
CD D:GLU144 3.1 6.2 1.0
CG D:HIS147 3.2 5.4 1.0
OE2 D:GLU114 3.3 16.6 1.0
CE1 D:HIS147 3.3 6.4 1.0
C D:ACY1 3.3 36.5 1.0
O D:ACY1 3.3 37.2 1.0
FE D:FE3 3.5 18.7 1.0
OE2 D:GLU144 3.5 6.6 1.0
CB D:HIS147 3.5 6.8 1.0
OE1 D:GLU243 3.9 28.6 1.0
HD1 D:HIS246 4.0 0.0 1.0
CG D:GLU114 4.2 9.7 1.0
NE2 D:HIS147 4.4 6.2 1.0
CD2 D:HIS147 4.4 9.0 1.0
OE2 D:GLU243 4.4 19.4 1.0
CE1 D:HIS246 4.5 16.7 1.0
CG D:GLU144 4.5 2.0 1.0
CA D:GLU114 4.6 10.2 1.0
CB D:GLU114 4.6 10.3 1.0
CD D:GLU243 4.6 22.7 1.0
ND1 D:HIS246 4.6 17.9 1.0
CG2 D:ILE239 4.7 9.3 1.0
CA D:GLU144 4.7 6.2 1.0
CH3 D:ACY1 4.7 38.5 1.0
CB D:GLU144 4.9 5.5 1.0
O D:ASP143 5.0 8.3 1.0

Iron binding site 3 out of 4 in 1mmo

Go back to Iron Binding Sites List in 1mmo
Iron binding site 3 out of 4 in the Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe1

b:21.2
occ:1.00
 HD1 E:HIS246 1.2 0.0 1.0
H2 E:HOH630 1.9 0.0 1.0
OE2 E:GLU209 1.9 26.0 1.0
OE2 E:GLU243 2.0 14.9 1.0
O E:ACY527 2.0 21.9 1.0
O E:HOH630 2.1 7.0 1.0
ND1 E:HIS246 2.2 11.7 1.0
H1 E:HOH630 2.4 0.0 1.0
OE2 E:GLU144 2.6 7.2 1.0
CD E:GLU209 2.9 22.8 1.0
CD E:GLU243 3.0 22.1 1.0
CE1 E:HIS246 3.0 11.2 1.0
C E:ACY527 3.0 20.6 1.0
CG E:HIS246 3.2 12.7 1.0
OE1 E:GLU243 3.3 25.2 1.0
OXT E:ACY527 3.3 17.4 1.0
FE E:FE2 3.4 15.7 1.0
HE22 E:GLN140 3.5 0.0 1.0
CD E:GLU144 3.6 13.1 1.0
CG E:GLU209 3.6 16.8 1.0
CB E:HIS246 3.7 13.8 1.0
OE1 E:GLU144 3.8 14.3 1.0
OE1 E:GLU209 3.9 27.0 1.0
NE2 E:GLN140 3.9 16.8 1.0
H1 E:HOH629 4.0 0.0 1.0
HD1 E:HIS147 4.0 0.0 1.0
NE2 E:HIS246 4.2 12.9 1.0
HE21 E:GLN140 4.2 0.0 1.0
O E:HOH629 4.3 15.8 1.0
CH3 E:ACY527 4.3 17.7 1.0
CD2 E:HIS246 4.3 10.4 1.0
CG E:GLU243 4.3 17.1 1.0
CB E:GLU209 4.6 14.3 1.0
ND1 E:HIS147 4.7 7.1 1.0
CE1 E:HIS147 4.7 7.8 1.0
CD E:GLN140 4.7 13.8 1.0
H2 E:HOH629 4.7 0.0 1.0
CG E:GLU144 4.9 4.9 1.0
CG E:GLN140 5.0 12.6 1.0

Iron binding site 4 out of 4 in 1mmo

Go back to Iron Binding Sites List in 1mmo
Iron binding site 4 out of 4 in the Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe2

b:15.7
occ:1.00
 HD1 E:HIS147 1.2 0.0 1.0
H2 E:HOH630 1.5 0.0 1.0
O E:HOH630 1.7 7.0 1.0
H1 E:HOH630 1.8 0.0 1.0
OXT E:ACY527 1.9 17.4 1.0
OE1 E:GLU114 2.0 13.8 1.0
H1 E:HOH629 2.0 0.0 1.0
OE1 E:GLU144 2.1 14.3 1.0
ND1 E:HIS147 2.2 7.1 1.0
O E:HOH629 2.4 15.8 1.0
C E:ACY527 2.9 20.6 1.0
CD E:GLU114 3.0 16.7 1.0
CD E:GLU144 3.1 13.1 1.0
CE1 E:HIS147 3.2 7.8 1.0
O E:ACY527 3.2 21.9 1.0
H2 E:HOH629 3.2 0.0 1.0
CG E:HIS147 3.2 8.9 1.0
FE E:FE1 3.4 21.2 1.0
OE2 E:GLU144 3.4 7.2 1.0
OE2 E:GLU114 3.5 23.3 1.0
CB E:HIS147 3.6 5.2 1.0
HD1 E:HIS246 4.0 0.0 1.0
OE1 E:GLU243 4.0 25.2 1.0
CH3 E:ACY527 4.3 17.7 1.0
NE2 E:HIS147 4.3 5.9 1.0
CG E:GLU114 4.3 14.1 1.0
CD2 E:HIS147 4.4 4.6 1.0
CE1 E:HIS246 4.4 11.2 1.0
CG E:GLU144 4.5 4.9 1.0
OE2 E:GLU243 4.5 14.9 1.0
CA E:GLU114 4.6 10.3 1.0
ND1 E:HIS246 4.6 11.7 1.0
CB E:GLU114 4.6 8.8 1.0
CG2 E:ILE239 4.7 10.4 1.0
CD E:GLU243 4.7 22.1 1.0
CA E:GLU144 4.7 8.2 1.0
CB E:GLU144 5.0 6.6 1.0
OE2 E:GLU209 5.0 26.0 1.0

Reference:

A.C.Rosenzweig, C.A.Frederick, S.J.Lippard, P.Nordlund. Crystal Structure of A Bacterial Non-Haem Iron Hydroxylase That Catalyses the Biological Oxidation of Methane. Nature V. 366 537 1993.
ISSN: ISSN 0028-0836
PubMed: 8255292
DOI: 10.1038/366537A0
Page generated: Sat Aug 3 11:01:56 2024

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