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Iron in PDB 2qd5: Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound

Enzymatic activity of Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound

All present enzymatic activity of Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound:
4.99.1.1;

Protein crystallography data

The structure of Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound, PDB code: 2qd5 was solved by A.E.Meldock, 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) 47.26 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 86.218, 92.811, 109.808, 90.00, 90.00, 90.00
R / Rfree (%) 23.7 / 28

Other elements in 2qd5:

The structure of Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound also contains other interesting chemical elements:

Lead (Pb) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound (pdb code 2qd5). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound, PDB code: 2qd5:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 2qd5

Go back to Iron Binding Sites List in 2qd5
Iron binding site 1 out of 4 in the Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:56.9
occ:1.00
 FE1 A:FES501 0.0 56.9 1.0
S2 A:FES501 2.2 55.8 1.0
S1 A:FES501 2.2 57.0 1.0
SG A:CYS411 2.3 58.4 1.0
SG A:CYS406 2.3 58.5 1.0
FE2 A:FES501 2.7 56.0 1.0
CB A:CYS411 3.3 59.3 1.0
CB A:CYS406 3.4 60.1 1.0
CA A:CYS406 4.3 60.9 1.0
CB A:ASN408 4.3 63.5 1.0
SG A:CYS196 4.4 50.9 1.0
SG A:CYS403 4.5 57.3 1.0
CB A:CYS403 4.6 56.4 1.0
N A:CYS403 4.7 55.6 1.0
CA A:CYS411 4.7 60.3 1.0
CB A:SER402 4.7 54.4 1.0
O A:ASN408 4.7 63.5 1.0
OG A:SER402 4.8 56.2 1.0
C A:CYS406 5.0 61.4 1.0
N A:ASN408 5.0 63.6 1.0

Iron binding site 2 out of 4 in 2qd5

Go back to Iron Binding Sites List in 2qd5
Iron binding site 2 out of 4 in the Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:56.0
occ:1.00
 FE2 A:FES501 0.0 56.0 1.0
S1 A:FES501 2.2 57.0 1.0
S2 A:FES501 2.3 55.8 1.0
SG A:CYS196 2.3 50.9 1.0
SG A:CYS403 2.3 57.3 1.0
FE1 A:FES501 2.7 56.9 1.0
CB A:CYS196 3.4 45.6 1.0
CB A:CYS403 3.4 56.4 1.0
O A:HOH1119 3.8 45.7 1.0
N A:CYS403 3.9 55.6 1.0
CA A:CYS403 4.2 56.8 1.0
SG A:CYS411 4.5 58.4 1.0
SG A:CYS406 4.5 58.5 1.0
CB A:CYS406 4.6 60.1 1.0
CA A:CYS196 4.7 41.6 1.0
C A:SER402 5.0 54.5 1.0

Iron binding site 3 out of 4 in 2qd5

Go back to Iron Binding Sites List in 2qd5
Iron binding site 3 out of 4 in the Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:55.7
occ:1.00
 FE1 B:FES502 0.0 55.7 1.0
S1 B:FES502 2.2 54.3 1.0
S2 B:FES502 2.2 54.3 1.0
SG B:CYS911 2.3 55.5 1.0
SG B:CYS906 2.3 56.7 1.0
FE2 B:FES502 2.7 53.9 1.0
CB B:CYS911 3.3 56.1 1.0
CB B:CYS906 3.4 57.6 1.0
OG B:SER902 4.0 57.5 1.0
CA B:CYS906 4.3 58.3 1.0
SG B:CYS696 4.4 49.8 1.0
CB B:ASN908 4.5 59.4 1.0
SG B:CYS903 4.5 55.0 1.0
CB B:CYS903 4.6 54.9 1.0
O B:ASN908 4.6 60.0 1.0
N B:CYS903 4.7 54.6 1.0
CA B:CYS911 4.7 56.9 1.0
CB B:CYS696 4.9 44.2 1.0
N B:ASN908 4.9 59.8 1.0
N B:VAL907 5.0 59.1 1.0

Iron binding site 4 out of 4 in 2qd5

Go back to Iron Binding Sites List in 2qd5
Iron binding site 4 out of 4 in the Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of Wild Type Human Ferrochelatase in Complex with A Lead- Porphyrin Compound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:53.9
occ:1.00
 FE2 B:FES502 0.0 53.9 1.0
S1 B:FES502 2.2 54.3 1.0
S2 B:FES502 2.2 54.3 1.0
SG B:CYS696 2.3 49.8 1.0
SG B:CYS903 2.3 55.0 1.0
FE1 B:FES502 2.7 55.7 1.0
O B:HOH1173 3.2 50.8 1.0
CB B:CYS696 3.4 44.2 1.0
CB B:CYS903 3.4 54.9 1.0
N B:CYS903 4.0 54.6 1.0
CA B:CYS903 4.2 55.0 1.0
SG B:CYS911 4.5 55.5 1.0
SG B:CYS906 4.5 56.7 1.0
CB B:CYS906 4.6 57.6 1.0
CA B:CYS696 4.8 40.2 1.0
OD1 B:ASP774 4.9 37.9 1.0
OG B:SER902 4.9 57.5 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: Thu Jul 17 03:39:49 2025

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