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Iron in PDB 4dl1: Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog

Enzymatic activity of Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog

All present enzymatic activity of Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog:
1.11.2.2;

Protein crystallography data

The structure of Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog, PDB code: 4dl1 was solved by F.Vajdos, A.Varghese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 128.49 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 63.829, 242.636, 151.505, 90.00, 91.19, 90.00
R / Rfree (%) 19 / 24.6

Other elements in 4dl1:

The structure of Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog also contains other interesting chemical elements:

Chlorine (Cl) 8 atoms
Calcium (Ca) 8 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog (pdb code 4dl1). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog, PDB code: 4dl1:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in 4dl1

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Iron binding site 1 out of 8 in the Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog


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 Human Myeloperoxidase with Covalent Thioxanthine Analog within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe601

b:18.3
occ:1.00
FE C:HEM601 0.0 18.3 1.0
NB C:HEM601 2.0 15.8 1.0
NA C:HEM601 2.0 13.6 1.0
NC C:HEM601 2.1 12.8 1.0
ND C:HEM601 2.1 15.9 1.0
NE2 C:HIS336 2.2 20.4 1.0
O A:HOH1701 2.9 19.1 1.0
C1B C:HEM601 3.0 19.5 1.0
C4B C:HEM601 3.0 15.2 1.0
C4D C:HEM601 3.0 13.6 1.0
C1D C:HEM601 3.1 11.5 1.0
C1A C:HEM601 3.1 20.1 1.0
C4A C:HEM601 3.1 17.5 1.0
C1C C:HEM601 3.1 11.8 1.0
C4C C:HEM601 3.1 13.6 1.0
CE1 C:HIS336 3.2 20.5 1.0
CD2 C:HIS336 3.2 15.7 1.0
CHA C:HEM601 3.4 18.6 1.0
CHC C:HEM601 3.4 13.8 1.0
CHB C:HEM601 3.4 17.4 1.0
CHD C:HEM601 3.5 16.0 1.0
C2B C:HEM601 4.2 17.4 1.0
C3B C:HEM601 4.2 19.8 1.0
C2D C:HEM601 4.3 13.3 1.0
C3D C:HEM601 4.3 17.2 1.0
C3A C:HEM601 4.3 16.6 1.0
C2A C:HEM601 4.3 16.8 1.0
ND1 C:HIS336 4.3 21.9 1.0
C3C C:HEM601 4.3 13.7 1.0
C2C C:HEM601 4.3 18.4 1.0
CG C:HIS336 4.3 12.6 1.0
CD2 C:LEU417 4.7 10.9 1.0
NE2 A:GLN91 4.8 15.0 1.0
CG C:ARG333 4.9 12.2 1.0

Iron binding site 2 out of 8 in 4dl1

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Iron binding site 2 out of 8 in the Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog


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 Human Myeloperoxidase with Covalent Thioxanthine Analog within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe202

b:22.9
occ:1.00
FE B:HEM202 0.0 22.9 1.0
ND B:HEM202 2.0 22.6 1.0
NB B:HEM202 2.1 24.5 1.0
NC B:HEM202 2.1 20.9 1.0
NA B:HEM202 2.1 21.8 1.0
NE2 D:HIS336 2.2 25.9 1.0
O B:HOH354 2.7 8.0 1.0
C1D B:HEM202 3.0 18.4 1.0
C1B B:HEM202 3.0 22.2 1.0
C4D B:HEM202 3.0 21.0 1.0
C4C B:HEM202 3.1 19.1 1.0
C4B B:HEM202 3.1 24.6 1.0
C4A B:HEM202 3.1 22.4 1.0
C1C B:HEM202 3.1 19.6 1.0
C1A B:HEM202 3.1 23.6 1.0
CE1 D:HIS336 3.2 24.2 1.0
CD2 D:HIS336 3.2 23.1 1.0
CHD B:HEM202 3.4 19.1 1.0
CHB B:HEM202 3.4 23.0 1.0
CHA B:HEM202 3.5 21.7 1.0
CHC B:HEM202 3.5 18.9 1.0
C2D B:HEM202 4.2 18.5 1.0
C3D B:HEM202 4.2 19.1 1.0
C2B B:HEM202 4.2 24.2 1.0
C3B B:HEM202 4.3 24.1 1.0
ND1 D:HIS336 4.3 22.1 1.0
C3C B:HEM202 4.3 15.5 1.0
CG D:HIS336 4.3 27.0 1.0
C3A B:HEM202 4.3 24.9 1.0
C2C B:HEM202 4.3 19.4 1.0
C2A B:HEM202 4.4 27.6 1.0
CD2 D:LEU417 4.7 25.7 1.0
O B:HOH366 4.9 16.5 1.0
O D:HOH721 5.0 24.2 1.0

Iron binding site 3 out of 8 in 4dl1

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Iron binding site 3 out of 8 in the Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog


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 Human Myeloperoxidase with Covalent Thioxanthine Analog within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe1602

b:22.7
occ:1.00
FE E:HEM1602 0.0 22.7 1.0
NB E:HEM1602 2.0 20.3 1.0
ND E:HEM1602 2.0 18.5 1.0
NC E:HEM1602 2.0 20.3 1.0
NA E:HEM1602 2.1 19.9 1.0
NE2 G:HIS336 2.2 19.4 1.0
O E:HOH1703 2.9 23.5 1.0
C1B E:HEM1602 3.0 20.0 1.0
C1D E:HEM1602 3.0 17.3 1.0
C4B E:HEM1602 3.0 22.2 1.0
C4C E:HEM1602 3.0 20.5 1.0
C4D E:HEM1602 3.1 13.9 1.0
C1C E:HEM1602 3.1 19.8 1.0
C4A E:HEM1602 3.1 20.3 1.0
CD2 G:HIS336 3.1 20.9 1.0
C1A E:HEM1602 3.1 13.1 1.0
CE1 G:HIS336 3.2 24.1 1.0
CHD E:HEM1602 3.3 15.2 1.0
CHB E:HEM1602 3.4 17.6 1.0
CHC E:HEM1602 3.4 22.9 1.0
CHA E:HEM1602 3.5 13.3 1.0
C3B E:HEM1602 4.2 15.3 1.0
C2B E:HEM1602 4.2 20.0 1.0
C2D E:HEM1602 4.2 14.2 1.0
C3C E:HEM1602 4.2 21.0 1.0
C3D E:HEM1602 4.3 15.1 1.0
C2C E:HEM1602 4.3 23.8 1.0
CG G:HIS336 4.3 20.4 1.0
ND1 G:HIS336 4.3 26.2 1.0
C3A E:HEM1602 4.3 17.1 1.0
C2A E:HEM1602 4.4 17.7 1.0
CD2 G:LEU417 4.7 15.6 1.0
NE2 E:GLN91 4.8 28.3 1.0

Iron binding site 4 out of 8 in 4dl1

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Iron binding site 4 out of 8 in the Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog


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 Human Myeloperoxidase with Covalent Thioxanthine Analog within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe202

b:29.9
occ:1.00
FE F:HEM202 0.0 29.9 1.0
NB F:HEM202 2.0 29.8 1.0
NA F:HEM202 2.1 30.8 1.0
ND F:HEM202 2.1 26.5 1.0
NC F:HEM202 2.2 26.2 1.0
NE2 H:HIS336 2.2 30.6 1.0
O F:HOH307 2.9 28.3 1.0
C1B F:HEM202 3.0 30.6 1.0
C4B F:HEM202 3.0 30.9 1.0
C4A F:HEM202 3.1 28.1 1.0
C1D F:HEM202 3.1 23.6 1.0
C4D F:HEM202 3.1 30.0 1.0
C1A F:HEM202 3.1 32.6 1.0
C4C F:HEM202 3.1 25.9 1.0
C1C F:HEM202 3.2 25.8 1.0
CD2 H:HIS336 3.2 28.2 1.0
CE1 H:HIS336 3.2 30.5 1.0
CHB F:HEM202 3.4 30.9 1.0
CHD F:HEM202 3.4 24.7 1.0
CHA F:HEM202 3.5 32.8 1.0
CHC F:HEM202 3.5 32.1 1.0
C2B F:HEM202 4.2 28.1 1.0
C3B F:HEM202 4.2 29.7 1.0
C2D F:HEM202 4.3 25.3 1.0
C3D F:HEM202 4.3 26.0 1.0
C3A F:HEM202 4.3 30.5 1.0
ND1 H:HIS336 4.3 26.6 1.0
C2A F:HEM202 4.3 31.7 1.0
CG H:HIS336 4.3 30.1 1.0
C3C F:HEM202 4.4 22.6 1.0
C2C F:HEM202 4.4 26.9 1.0
NE2 F:GLN91 4.9 27.3 1.0
CD2 H:LEU417 4.9 32.4 1.0

Iron binding site 5 out of 8 in 4dl1

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Iron binding site 5 out of 8 in the Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Fe1602

b:20.3
occ:1.00
FE I:HEM1602 0.0 20.3 1.0
NB I:HEM1602 2.0 16.0 1.0
NC I:HEM1602 2.1 15.9 1.0
ND I:HEM1602 2.1 22.0 1.0
NA I:HEM1602 2.2 14.8 1.0
NE2 K:HIS336 2.2 22.1 1.0
O I:HOH1770 2.7 8.5 1.0
C1B I:HEM1602 3.0 21.5 1.0
C4B I:HEM1602 3.1 21.8 1.0
C1D I:HEM1602 3.1 19.3 1.0
C4C I:HEM1602 3.1 17.3 1.0
C1C I:HEM1602 3.1 18.0 1.0
C4D I:HEM1602 3.1 20.6 1.0
C4A I:HEM1602 3.1 17.8 1.0
C1A I:HEM1602 3.2 23.1 1.0
CD2 K:HIS336 3.2 12.8 1.0
CE1 K:HIS336 3.2 17.3 1.0
CHD I:HEM1602 3.4 17.9 1.0
CHB I:HEM1602 3.4 21.0 1.0
CHC I:HEM1602 3.4 22.1 1.0
CHA I:HEM1602 3.5 19.5 1.0
C2B I:HEM1602 4.2 16.8 1.0
C3B I:HEM1602 4.3 20.1 1.0
C2D I:HEM1602 4.3 21.6 1.0
ND1 K:HIS336 4.3 19.6 1.0
C2C I:HEM1602 4.3 18.5 1.0
C3C I:HEM1602 4.3 15.8 1.0
C3D I:HEM1602 4.3 19.8 1.0
CG K:HIS336 4.3 19.1 1.0
C3A I:HEM1602 4.4 21.4 1.0
C2A I:HEM1602 4.4 22.6 1.0
CD2 K:LEU417 4.8 19.5 1.0

Iron binding site 6 out of 8 in 4dl1

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Iron binding site 6 out of 8 in the Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Fe202

b:24.7
occ:1.00
FE J:HEM202 0.0 24.7 1.0
NB J:HEM202 2.0 21.4 1.0
NC J:HEM202 2.1 24.7 1.0
NA J:HEM202 2.1 26.3 1.0
ND J:HEM202 2.2 22.6 1.0
NE2 L:HIS336 2.2 23.8 1.0
O J:HOH302 2.9 23.1 1.0
C1B J:HEM202 3.0 23.4 1.0
C4B J:HEM202 3.1 24.1 1.0
CE1 L:HIS336 3.1 23.8 1.0
C4D J:HEM202 3.1 23.4 1.0
C4C J:HEM202 3.1 25.0 1.0
C1C J:HEM202 3.1 22.0 1.0
C1A J:HEM202 3.1 28.1 1.0
C1D J:HEM202 3.1 25.7 1.0
C4A J:HEM202 3.1 28.8 1.0
CD2 L:HIS336 3.2 20.1 1.0
CHC J:HEM202 3.4 24.3 1.0
CHA J:HEM202 3.5 25.2 1.0
CHB J:HEM202 3.5 23.9 1.0
CHD J:HEM202 3.5 25.4 1.0
ND1 L:HIS336 4.2 24.2 1.0
C2B J:HEM202 4.2 23.6 1.0
C3B J:HEM202 4.3 24.4 1.0
C2C J:HEM202 4.3 22.5 1.0
C3C J:HEM202 4.3 22.2 1.0
C3D J:HEM202 4.3 20.0 1.0
C2D J:HEM202 4.3 21.8 1.0
CG L:HIS336 4.3 25.8 1.0
C2A J:HEM202 4.3 28.4 1.0
C3A J:HEM202 4.4 27.2 1.0
CD2 L:LEU417 4.7 26.3 1.0
O J:HOH349 4.9 46.9 1.0
NE2 J:GLN91 4.9 21.8 1.0
CG J:GLN91 4.9 20.0 1.0
O L:HOH794 5.0 30.6 1.0

Iron binding site 7 out of 8 in 4dl1

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Iron binding site 7 out of 8 in the Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Fe1602

b:24.5
occ:1.00
FE M:HEM1602 0.0 24.5 1.0
NB M:HEM1602 2.0 20.8 1.0
NA M:HEM1602 2.1 25.3 1.0
ND M:HEM1602 2.1 25.2 1.0
NC M:HEM1602 2.1 20.9 1.0
NE2 O:HIS336 2.2 23.9 1.0
O M:HOH1713 2.9 26.6 1.0
C1B M:HEM1602 3.0 26.1 1.0
C4B M:HEM1602 3.0 24.6 1.0
C4D M:HEM1602 3.0 21.7 1.0
C1A M:HEM1602 3.1 25.9 1.0
C1D M:HEM1602 3.1 25.1 1.0
C4A M:HEM1602 3.1 26.6 1.0
C4C M:HEM1602 3.1 19.1 1.0
C1C M:HEM1602 3.1 23.2 1.0
CE1 O:HIS336 3.2 24.6 1.0
CD2 O:HIS336 3.2 23.7 1.0
CHA M:HEM1602 3.4 25.2 1.0
CHB M:HEM1602 3.4 27.6 1.0
CHC M:HEM1602 3.5 22.9 1.0
CHD M:HEM1602 3.5 19.3 1.0
C2B M:HEM1602 4.2 23.7 1.0
C3B M:HEM1602 4.2 28.6 1.0
C3D M:HEM1602 4.3 24.8 1.0
C2D M:HEM1602 4.3 24.8 1.0
C2A M:HEM1602 4.3 26.3 1.0
ND1 O:HIS336 4.3 30.0 1.0
C3A M:HEM1602 4.3 27.5 1.0
CG O:HIS336 4.3 22.7 1.0
C3C M:HEM1602 4.3 22.0 1.0
C2C M:HEM1602 4.4 23.3 1.0
CD2 O:LEU417 4.7 18.9 1.0
NE2 M:GLN91 4.8 17.3 1.0

Iron binding site 8 out of 8 in 4dl1

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Iron binding site 8 out of 8 in the Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Crystal Structure of Human Myeloperoxidase with Covalent Thioxanthine Analog within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Fe202

b:29.3
occ:1.00
FE N:HEM202 0.0 29.3 1.0
NA N:HEM202 2.1 32.5 1.0
NC N:HEM202 2.1 26.4 1.0
NB N:HEM202 2.1 33.5 1.0
ND N:HEM202 2.1 29.5 1.0
NE2 P:HIS336 2.2 32.4 1.0
O N:HOH307 2.9 25.2 1.0
C4D N:HEM202 3.0 30.5 1.0
C4B N:HEM202 3.1 31.3 1.0
C1A N:HEM202 3.1 32.7 1.0
C1D N:HEM202 3.1 26.3 1.0
C1C N:HEM202 3.1 24.3 1.0
C1B N:HEM202 3.1 35.6 1.0
C4C N:HEM202 3.1 26.2 1.0
C4A N:HEM202 3.1 34.6 1.0
CD2 P:HIS336 3.2 33.8 1.0
CE1 P:HIS336 3.2 32.8 1.0
CHA N:HEM202 3.4 30.5 1.0
CHC N:HEM202 3.4 27.4 1.0
CHD N:HEM202 3.5 26.6 1.0
CHB N:HEM202 3.5 34.1 1.0
C3D N:HEM202 4.3 28.9 1.0
C3B N:HEM202 4.3 33.2 1.0
C2D N:HEM202 4.3 29.3 1.0
C2A N:HEM202 4.3 34.8 1.0
ND1 P:HIS336 4.3 33.9 1.0
C2B N:HEM202 4.3 32.6 1.0
C2C N:HEM202 4.3 21.3 1.0
C3C N:HEM202 4.3 25.9 1.0
C3A N:HEM202 4.3 36.7 1.0
CG P:HIS336 4.3 32.0 1.0
NE2 N:GLN91 4.8 21.9 1.0

Reference:

K.F.Geoghegan, A.H.Varghese, X.Feng, A.J.Bessire, J.J.Conboy, R.B.Ruggeri, K.Ahn, S.N.Spath, S.V.Filippov, S.J.Conrad, P.A.Carpino, C.R.Guimaraes, F.F.Vajdos. Deconstruction of Activity-Dependent Covalent Modification of Heme in Human Neutrophil Myeloperoxidase By Multistage Mass Spectrometry (Ms(4)). Biochemistry V. 51 2065 2012.
ISSN: ISSN 0006-2960
PubMed: 22352991
DOI: 10.1021/BI201872J
Page generated: Mon Aug 5 01:18:48 2024

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