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Iron in PDB 4klc: E343D/F110A Double Mutant of Human Ferrochelatase

Enzymatic activity of E343D/F110A Double Mutant of Human Ferrochelatase

All present enzymatic activity of E343D/F110A Double Mutant of Human Ferrochelatase:
4.99.1.1;

Protein crystallography data

The structure of E343D/F110A Double Mutant of Human Ferrochelatase, PDB code: 4klc was solved by W.N.Lanzilotta, A.E.Medlock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 136.78 / 2.40
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 62.659, 133.404, 136.781, 90.00, 90.00, 90.00
R / Rfree (%) 25.5 / 29.9

Iron Binding Sites:

The binding sites of Iron atom in the E343D/F110A Double Mutant of Human Ferrochelatase (pdb code 4klc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 6 binding sites of Iron where determined in the E343D/F110A Double Mutant of Human Ferrochelatase, PDB code: 4klc:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6;

Iron binding site 1 out of 6 in 4klc

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Iron binding site 1 out of 6 in the E343D/F110A Double Mutant of Human Ferrochelatase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of E343D/F110A Double Mutant of Human Ferrochelatase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:29.8
occ:1.00
 FE1 A:FES501 0.0 29.8 1.0
S2 A:FES501 2.2 28.9 1.0
SG A:CYS411 2.3 32.3 1.0
S1 A:FES501 2.3 24.2 1.0
SG A:CYS406 2.3 31.6 1.0
FE2 A:FES501 2.6 24.0 1.0
CB A:CYS411 3.1 33.4 1.0
CB A:CYS406 3.4 33.4 1.0
O A:HOH618 4.2 48.0 1.0
CB A:ASN408 4.3 36.5 1.0
O A:HOH708 4.3 23.5 1.0
CA A:CYS406 4.4 33.9 1.0
SG A:CYS196 4.4 27.2 1.0
O A:HOH646 4.5 26.8 1.0
O A:ASN408 4.5 36.3 1.0
SG A:CYS403 4.6 24.2 1.0
CA A:CYS411 4.6 33.6 1.0
O A:HOH648 4.6 28.9 1.0
N A:CYS403 4.8 27.5 1.0
OG A:SER402 4.8 35.3 1.0
CB A:SER402 4.9 30.4 1.0
CB A:CYS196 4.9 23.0 1.0
ND2 A:ASN408 4.9 41.5 1.0
N A:ASN408 4.9 36.3 1.0
O A:HOH762 5.0 35.1 1.0

Iron binding site 2 out of 6 in 4klc

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Iron binding site 2 out of 6 in the E343D/F110A Double Mutant of Human Ferrochelatase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of E343D/F110A Double Mutant of Human Ferrochelatase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:24.0
occ:1.00
 FE2 A:FES501 0.0 24.0 1.0
S1 A:FES501 2.2 24.2 1.0
S2 A:FES501 2.2 28.9 1.0
SG A:CYS196 2.3 27.2 1.0
SG A:CYS403 2.3 24.2 1.0
FE1 A:FES501 2.6 29.8 1.0
O A:HOH762 3.0 35.1 1.0
CB A:CYS196 3.5 23.0 1.0
CB A:CYS403 3.6 26.1 1.0
N A:CYS403 3.7 27.5 1.0
CA A:CYS403 4.3 26.9 1.0
SG A:CYS406 4.4 31.6 1.0
SG A:CYS411 4.4 32.3 1.0
CB A:CYS406 4.5 33.4 1.0
O A:HOH618 4.7 48.0 1.0
C A:SER402 4.8 28.7 1.0
CA A:CYS196 4.8 23.7 1.0
NH2 B:ARG298 4.9 29.8 1.0
NH1 A:ARG272 5.0 39.5 1.0

Iron binding site 3 out of 6 in 4klc

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Iron binding site 3 out of 6 in the E343D/F110A Double Mutant of Human Ferrochelatase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of E343D/F110A Double Mutant of Human Ferrochelatase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:35.2
occ:0.50
 FE A:HEM502 0.0 35.2 0.5
NA A:HEM502 2.0 34.2 0.5
NE2 A:HIS263 2.0 38.3 1.0
NB A:HEM502 2.1 33.7 0.5
ND A:HEM502 2.1 33.9 0.5
NC A:HEM502 2.2 33.4 0.5
CE1 A:HIS263 2.8 37.9 1.0
CD2 A:HIS263 2.9 37.7 1.0
C4A A:HEM502 3.0 34.0 0.5
C1B A:HEM502 3.0 33.2 0.5
C1A A:HEM502 3.1 33.9 0.5
C1D A:HEM502 3.1 33.8 0.5
C4B A:HEM502 3.1 33.6 0.5
C1C A:HEM502 3.1 33.1 0.5
C4D A:HEM502 3.2 33.0 0.5
C4C A:HEM502 3.2 33.7 0.5
CHB A:HEM502 3.3 32.7 0.5
CHD A:HEM502 3.5 34.1 0.5
CHA A:HEM502 3.5 34.3 0.5
CHC A:HEM502 3.5 33.1 0.5
ND1 A:HIS263 3.8 37.5 1.0
CG A:HIS263 3.9 34.5 1.0
C2B A:HEM502 4.2 32.6 0.5
C3A A:HEM502 4.2 34.4 0.5
SD A:MET76 4.2 34.3 0.5
C3B A:HEM502 4.3 32.7 0.5
C2A A:HEM502 4.3 33.9 0.5
C2C A:HEM502 4.3 33.9 0.5
C2D A:HEM502 4.4 33.5 0.5
C3C A:HEM502 4.4 33.3 0.5
CE A:MET76 4.4 28.2 0.5
C3D A:HEM502 4.4 31.9 0.5

Iron binding site 4 out of 6 in 4klc

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Iron binding site 4 out of 6 in the E343D/F110A Double Mutant of Human Ferrochelatase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of E343D/F110A Double Mutant of Human Ferrochelatase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:33.0
occ:1.00
 FE1 B:FES501 0.0 33.0 1.0
S2 B:FES501 2.2 31.1 1.0
S1 B:FES501 2.2 30.2 1.0
SG B:CYS411 2.3 37.2 1.0
SG B:CYS406 2.3 36.5 1.0
FE2 B:FES501 2.6 29.6 1.0
CB B:CYS411 3.2 37.2 1.0
CB B:CYS406 3.3 34.7 1.0
CA B:CYS406 4.2 35.5 1.0
CB B:ASN408 4.3 38.9 1.0
SG B:CYS196 4.4 31.1 1.0
O B:ASN408 4.5 39.4 1.0
SG B:CYS403 4.5 32.3 1.0
CA B:CYS411 4.6 37.1 1.0
O B:HOH649 4.8 39.3 1.0
N B:ASN408 4.8 38.9 1.0
N B:CYS403 4.8 28.6 1.0
CB B:SER402 4.8 28.0 1.0
CB B:CYS403 4.9 29.9 1.0
C B:CYS406 5.0 36.5 1.0
CB B:CYS196 5.0 23.2 1.0
N B:VAL407 5.0 37.1 1.0

Iron binding site 5 out of 6 in 4klc

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Iron binding site 5 out of 6 in the E343D/F110A Double Mutant of Human Ferrochelatase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of E343D/F110A Double Mutant of Human Ferrochelatase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:29.6
occ:1.00
 FE2 B:FES501 0.0 29.6 1.0
S1 B:FES501 2.2 30.2 1.0
S2 B:FES501 2.2 31.1 1.0
SG B:CYS196 2.3 31.1 1.0
SG B:CYS403 2.3 32.3 1.0
FE1 B:FES501 2.6 33.0 1.0
O B:HOH721 3.3 28.5 1.0
CB B:CYS403 3.4 29.9 1.0
CB B:CYS196 3.5 23.2 1.0
N B:CYS403 3.8 28.6 1.0
CA B:CYS403 4.2 29.7 1.0
SG B:CYS406 4.4 36.5 1.0
SG B:CYS411 4.4 37.2 1.0
CB B:CYS406 4.4 34.7 1.0
CA B:CYS196 4.8 23.1 1.0
NH1 B:ARG272 4.8 34.5 1.0
C B:SER402 4.9 28.3 1.0

Iron binding site 6 out of 6 in 4klc

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Iron binding site 6 out of 6 in the E343D/F110A Double Mutant of Human Ferrochelatase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of E343D/F110A Double Mutant of Human Ferrochelatase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe503

b:43.1
occ:0.50
 FE B:HEM503 0.0 43.1 0.5
NB B:HEM503 2.0 41.6 0.5
NE2 B:HIS263 2.0 39.3 1.0
NA B:HEM503 2.0 44.5 0.5
ND B:HEM503 2.1 42.5 0.5
NC B:HEM503 2.1 40.2 0.5
CD2 B:HIS263 2.8 36.4 1.0
CE1 B:HIS263 2.8 37.9 1.0
C1A B:HEM503 3.0 45.2 0.5
C1B B:HEM503 3.0 41.9 0.5
C4B B:HEM503 3.0 41.1 0.5
C4D B:HEM503 3.1 43.6 0.5
C1C B:HEM503 3.1 39.6 0.5
C4A B:HEM503 3.1 44.2 0.5
C4C B:HEM503 3.1 39.1 0.5
C1D B:HEM503 3.2 42.3 0.5
CHA B:HEM503 3.4 44.7 0.5
CHC B:HEM503 3.4 40.1 0.5
CHB B:HEM503 3.4 42.5 0.5
CHD B:HEM503 3.5 40.6 0.5
ND1 B:HIS263 3.7 37.2 1.0
CG B:HIS263 3.7 32.3 1.0
C3B B:HEM503 4.2 40.8 0.5
C2B B:HEM503 4.2 41.5 0.5
C2A B:HEM503 4.2 45.5 0.5
C3A B:HEM503 4.3 45.4 0.5
C2C B:HEM503 4.3 38.3 0.5
C3C B:HEM503 4.3 38.1 0.5
C3D B:HEM503 4.3 43.6 0.5
C2D B:HEM503 4.4 43.0 0.5
CE B:MET76 4.4 25.8 0.5
SD B:MET76 4.8 28.4 0.5
CB B:HIS263 5.0 25.1 1.0

Reference:

W.N.Lanzilotta, A.E.Medlock. E343D/F110A Double Mutant of Human Ferrochelatase To Be Published.
Page generated: Mon Aug 5 05:27:48 2024

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