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Iron in PDB 2qd3: Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate

Enzymatic activity of Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate

All present enzymatic activity of Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate:
4.99.1.1;

Protein crystallography data

The structure of Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate, PDB code: 2qd3 was solved by A.E.Medlock, T.A.Dailey, T.A.Ross, H.A.Dailey, W.N.Lanzilotta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.80 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 88.067, 93.088, 111.411, 90.00, 90.00, 90.00
R / Rfree (%) 20.9 / 24.2

Iron Binding Sites:

The binding sites of Iron atom in the Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate (pdb code 2qd3). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 5 binding sites of Iron where determined in the Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate, PDB code: 2qd3:
Jump to Iron binding site number: 1; 2; 3; 4; 5;

Iron binding site 1 out of 5 in 2qd3

Go back to Iron Binding Sites List in 2qd3
Iron binding site 1 out of 5 in the Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe601

b:23.6
occ:1.00
FE1 A:FES601 0.0 23.6 1.0
S2 A:FES601 2.2 23.4 1.0
S1 A:FES601 2.3 23.3 1.0
SG A:CYS411 2.3 24.6 1.0
SG A:CYS406 2.3 24.3 1.0
FE2 A:FES601 2.7 22.9 1.0
CB A:CYS411 3.2 25.3 1.0
CB A:CYS406 3.4 24.8 1.0
O A:HOH706 4.1 37.5 1.0
O A:HOH658 4.2 18.2 1.0
CA A:CYS406 4.3 25.1 1.0
O A:HOH699 4.3 33.7 1.0
SG A:CYS196 4.5 22.1 1.0
SG A:CYS403 4.6 23.5 1.0
CB A:ASN408 4.6 26.9 1.0
CA A:CYS411 4.7 25.9 1.0
N A:CYS403 4.7 22.8 1.0
CB A:CYS403 4.7 23.1 1.0
O A:ASN408 4.7 26.7 1.0
CB A:SER402 4.8 22.9 1.0
CB A:CYS196 5.0 20.4 1.0
N A:ASN408 5.0 26.7 1.0
OG A:SER402 5.0 23.8 1.0

Iron binding site 2 out of 5 in 2qd3

Go back to Iron Binding Sites List in 2qd3
Iron binding site 2 out of 5 in the Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe601

b:22.9
occ:1.00
FE2 A:FES601 0.0 22.9 1.0
S1 A:FES601 2.2 23.3 1.0
S2 A:FES601 2.3 23.4 1.0
SG A:CYS196 2.3 22.1 1.0
SG A:CYS403 2.3 23.5 1.0
FE1 A:FES601 2.7 23.6 1.0
CB A:CYS403 3.4 23.1 1.0
CB A:CYS196 3.4 20.4 1.0
O A:HOH682 3.8 39.7 1.0
N A:CYS403 3.9 22.8 1.0
CA A:CYS403 4.2 23.1 1.0
O A:HOH657 4.4 30.5 1.0
O A:HOH706 4.4 37.5 1.0
SG A:CYS411 4.5 24.6 1.0
SG A:CYS406 4.5 24.3 1.0
CB A:CYS406 4.6 24.8 1.0
CA A:CYS196 4.8 19.4 1.0
NE A:ARG272 4.8 19.7 0.5
CD A:ARG272 4.9 20.0 0.5
C A:SER402 5.0 22.6 1.0

Iron binding site 3 out of 5 in 2qd3

Go back to Iron Binding Sites List in 2qd3
Iron binding site 3 out of 5 in the Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe924

b:24.6
occ:1.00
FE1 B:FES924 0.0 24.6 1.0
S1 B:FES924 2.2 24.5 1.0
S2 B:FES924 2.2 24.3 1.0
SG B:CYS911 2.3 25.9 1.0
SG B:CYS906 2.3 25.2 1.0
FE2 B:FES924 2.7 24.1 1.0
CB B:CYS911 3.3 26.6 1.0
CB B:CYS906 3.4 25.5 1.0
O B:HOH1068 4.2 44.7 1.0
CA B:CYS906 4.2 25.6 1.0
O B:HOH1012 4.3 31.0 1.0
O B:HOH982 4.4 21.1 1.0
SG B:CYS696 4.5 23.6 1.0
SG B:CYS903 4.6 24.1 1.0
O B:ASN908 4.6 27.4 1.0
N B:CYS903 4.7 23.4 1.0
CB B:CYS903 4.7 23.8 1.0
CB B:ASN908 4.7 27.3 1.0
CA B:CYS911 4.7 27.2 1.0
CB B:SER902 4.8 23.5 1.0
CB B:CYS696 4.9 21.8 1.0

Iron binding site 4 out of 5 in 2qd3

Go back to Iron Binding Sites List in 2qd3
Iron binding site 4 out of 5 in the Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe924

b:24.1
occ:1.00
FE2 B:FES924 0.0 24.1 1.0
S1 B:FES924 2.2 24.5 1.0
S2 B:FES924 2.3 24.3 1.0
SG B:CYS903 2.3 24.1 1.0
SG B:CYS696 2.3 23.6 1.0
FE1 B:FES924 2.7 24.6 1.0
CB B:CYS903 3.4 23.8 1.0
CB B:CYS696 3.4 21.8 1.0
O B:HOH1013 3.7 36.6 1.0
N B:CYS903 3.8 23.4 1.0
CA B:CYS903 4.2 23.6 1.0
O B:HOH968 4.2 32.5 1.0
O B:HOH1068 4.3 44.7 1.0
SG B:CYS911 4.5 25.9 1.0
SG B:CYS906 4.5 25.2 1.0
CB B:CYS906 4.6 25.5 1.0
CA B:CYS696 4.8 20.9 1.0
NE B:ARG772 4.8 23.8 1.0
C B:SER902 5.0 23.2 1.0
NH2 A:ARG298 5.0 20.1 1.0

Iron binding site 5 out of 5 in 2qd3

Go back to Iron Binding Sites List in 2qd3
Iron binding site 5 out of 5 in the Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Wild Type Human Ferrochelatase Crystallized with Ammonium Sulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe925

b:30.9
occ:0.50
FE B:HEM925 0.0 30.9 0.5
NC B:HEM925 1.9 30.5 0.5
ND B:HEM925 1.9 30.5 0.5
NA B:HEM925 2.0 30.6 0.5
NB B:HEM925 2.0 30.5 0.5
C1D B:HEM925 2.9 30.5 0.5
C4D B:HEM925 3.0 30.5 0.5
C4C B:HEM925 3.0 30.5 0.5
C1C B:HEM925 3.0 30.4 0.5
C1B B:HEM925 3.0 30.5 0.5
C4B B:HEM925 3.0 30.6 0.5
C4A B:HEM925 3.0 30.7 0.5
C1A B:HEM925 3.0 30.6 0.5
CHD B:HEM925 3.3 30.5 0.5
CHA B:HEM925 3.4 30.5 0.5
CHC B:HEM925 3.4 30.5 0.5
CHB B:HEM925 3.4 30.6 0.5
CE1 B:HIS763 3.4 19.7 1.0
NE2 B:HIS763 3.7 19.8 1.0
ND1 B:HIS763 4.1 19.6 1.0
C2C B:HEM925 4.2 30.4 0.5
C3C B:HEM925 4.2 30.5 0.5
C2A B:HEM925 4.2 30.8 0.5
C2B B:HEM925 4.2 30.6 0.5
C3A B:HEM925 4.2 30.8 0.5
C2D B:HEM925 4.2 30.5 0.5
C3D B:HEM925 4.2 30.5 0.5
C3B B:HEM925 4.3 30.6 0.5
O B:HOH1105 4.3 42.4 1.0
CD2 B:HIS763 4.6 19.5 1.0
CG B:HIS763 4.9 19.4 1.0

Reference:

A.E.Medlock, T.A.Dailey, T.A.Ross, H.A.Dailey, W.N.Lanzilotta. A Pi-Helix Switch Selective For Porphyrin Deprotonation and Product Release in Human Ferrochelatase. J.Mol.Biol. V. 373 1006 2007.
ISSN: ISSN 0022-2836
PubMed: 17884090
DOI: 10.1016/J.JMB.2007.08.040
Page generated: Sun Dec 13 14:51:50 2020

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