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Iron in PDB 2p85: Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations

Enzymatic activity of Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations

All present enzymatic activity of Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations:
1.14.14.1;

Protein crystallography data

The structure of Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations, PDB code: 2p85 was solved by E.E.Scott, C.D.Stout, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.34 / 2.35
Space group P 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 121.320, 110.280, 142.000, 90.00, 110.28, 90.00
R / Rfree (%) 21.9 / 27.7

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations (pdb code 2p85). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 6 binding sites of Iron where determined in the Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations, PDB code: 2p85:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6;

Iron binding site 1 out of 6 in 2p85

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Iron binding site 1 out of 6 in the Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:20.0
occ:1.00
 FE A:HEM500 0.0 20.0 1.0
ND A:HEM500 2.1 16.3 1.0
NB A:HEM500 2.1 19.3 1.0
NA A:HEM500 2.1 23.9 1.0
NC A:HEM500 2.1 20.0 1.0
SG A:CYS439 2.3 25.0 1.0
C1D A:HEM500 3.0 18.5 1.0
C4B A:HEM500 3.0 27.7 1.0
C1C A:HEM500 3.0 17.9 1.0
C4D A:HEM500 3.0 28.6 1.0
C4A A:HEM500 3.0 19.6 1.0
C1B A:HEM500 3.1 27.3 1.0
C1A A:HEM500 3.1 19.4 1.0
C4C A:HEM500 3.1 21.6 1.0
CHC A:HEM500 3.3 26.7 1.0
CHB A:HEM500 3.3 20.7 1.0
CB A:CYS439 3.3 29.8 1.0
CHA A:HEM500 3.4 19.3 1.0
CHD A:HEM500 3.4 21.9 1.0
C2D A:HEM500 4.2 17.8 1.0
C3D A:HEM500 4.3 16.0 1.0
C2C A:HEM500 4.3 19.3 1.0
C3A A:HEM500 4.3 24.9 1.0
C2A A:HEM500 4.3 19.1 1.0
C3B A:HEM500 4.3 26.9 1.0
CA A:CYS439 4.3 28.0 1.0
C2B A:HEM500 4.3 28.4 1.0
C3C A:HEM500 4.3 24.1 1.0
C5 A:IND507 4.3 31.6 0.4
C4 A:IND507 4.5 31.6 0.4
C6 A:IND501 4.6 31.6 0.6
CB A:ALA301 4.7 20.1 1.0

Iron binding site 2 out of 6 in 2p85

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Iron binding site 2 out of 6 in the Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:22.1
occ:1.00
 FE B:HEM500 0.0 22.1 1.0
NA B:HEM500 2.0 17.2 1.0
ND B:HEM500 2.0 15.1 1.0
NC B:HEM500 2.1 17.3 1.0
NB B:HEM500 2.1 13.3 1.0
SG B:CYS439 2.5 25.1 1.0
C1D B:HEM500 3.0 22.8 1.0
C4B B:HEM500 3.0 15.3 1.0
C4D B:HEM500 3.0 22.5 1.0
C4A B:HEM500 3.0 24.8 1.0
C1C B:HEM500 3.0 24.2 1.0
C1A B:HEM500 3.0 27.2 1.0
C1B B:HEM500 3.1 16.6 1.0
C4C B:HEM500 3.1 17.3 1.0
CB B:CYS439 3.2 21.0 1.0
CHC B:HEM500 3.3 19.8 1.0
CHA B:HEM500 3.3 19.2 1.0
CHB B:HEM500 3.3 20.6 1.0
CHD B:HEM500 3.3 19.2 1.0
C2D B:HEM500 4.2 22.6 1.0
C3A B:HEM500 4.2 22.8 1.0
C2C B:HEM500 4.2 17.1 1.0
C3D B:HEM500 4.2 23.5 1.0
C2A B:HEM500 4.2 30.7 1.0
C3B B:HEM500 4.3 13.8 1.0
CA B:CYS439 4.3 28.5 1.0
C3C B:HEM500 4.3 16.6 1.0
C2B B:HEM500 4.3 9.5 1.0
C5 B:IND508 4.3 31.6 0.6
C4 B:IND508 4.7 31.6 0.6
CB B:ALA301 4.8 32.2 1.0

Iron binding site 3 out of 6 in 2p85

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Iron binding site 3 out of 6 in the Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe500

b:34.5
occ:1.00
 FE C:HEM500 0.0 34.5 1.0
ND C:HEM500 2.0 18.3 1.0
NB C:HEM500 2.1 22.8 1.0
NC C:HEM500 2.1 28.0 1.0
NA C:HEM500 2.1 36.8 1.0
SG C:CYS439 2.5 41.5 1.0
C1D C:HEM500 3.0 32.7 1.0
C4B C:HEM500 3.0 27.9 1.0
C1C C:HEM500 3.0 24.9 1.0
C4D C:HEM500 3.0 32.6 1.0
C4A C:HEM500 3.0 35.2 1.0
C1B C:HEM500 3.1 28.4 1.0
C4C C:HEM500 3.1 28.9 1.0
C1A C:HEM500 3.1 28.2 1.0
CHC C:HEM500 3.3 24.2 1.0
CHD C:HEM500 3.3 34.6 1.0
CHA C:HEM500 3.3 24.3 1.0
CHB C:HEM500 3.3 30.6 1.0
CB C:CYS439 3.4 39.4 1.0
C5 C:IND509 3.9 31.6 0.4
C2D C:HEM500 4.2 30.2 1.0
C2C C:HEM500 4.2 34.6 1.0
C3D C:HEM500 4.2 26.2 1.0
C3B C:HEM500 4.2 24.7 1.0
C3A C:HEM500 4.3 34.8 1.0
C3C C:HEM500 4.3 34.9 1.0
C2A C:HEM500 4.3 35.3 1.0
CA C:CYS439 4.3 35.8 1.0
C2B C:HEM500 4.3 12.3 1.0
C4 C:IND509 4.6 31.6 0.4
C6 C:IND509 4.7 31.6 0.4
C6 C:IND503 4.8 31.6 0.6
CB C:ALA301 4.8 45.2 1.0

Iron binding site 4 out of 6 in 2p85

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Iron binding site 4 out of 6 in the Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe500

b:26.4
occ:1.00
 FE D:HEM500 0.0 26.4 1.0
NA D:HEM500 2.0 24.4 1.0
NB D:HEM500 2.1 29.7 1.0
ND D:HEM500 2.1 22.4 1.0
NC D:HEM500 2.1 23.8 1.0
SG D:CYS439 2.5 31.5 1.0
C1C D:HEM500 3.0 28.3 1.0
C4B D:HEM500 3.0 23.3 1.0
C1D D:HEM500 3.0 20.3 1.0
C4A D:HEM500 3.0 29.3 1.0
C4D D:HEM500 3.0 24.2 1.0
C1A D:HEM500 3.0 26.5 1.0
C1B D:HEM500 3.0 31.7 1.0
C4C D:HEM500 3.1 24.9 1.0
CHC D:HEM500 3.3 28.0 1.0
CHB D:HEM500 3.3 31.3 1.0
CB D:CYS439 3.3 31.1 1.0
CHD D:HEM500 3.3 27.7 1.0
CHA D:HEM500 3.4 23.1 1.0
C5 D:IND510 3.8 31.6 0.5
C2C D:HEM500 4.2 27.8 1.0
C2D D:HEM500 4.2 21.2 1.0
C3A D:HEM500 4.2 23.3 1.0
C3D D:HEM500 4.2 21.4 1.0
C3B D:HEM500 4.2 29.9 1.0
C2A D:HEM500 4.2 27.9 1.0
C3C D:HEM500 4.3 19.9 1.0
C2B D:HEM500 4.3 31.1 1.0
CA D:CYS439 4.3 30.5 1.0
C4 D:IND510 4.5 31.6 0.5
C6 D:IND504 4.6 31.6 0.5
C6 D:IND510 4.6 31.6 0.5
CB D:ALA301 4.8 37.5 1.0

Iron binding site 5 out of 6 in 2p85

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Iron binding site 5 out of 6 in the Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe500

b:29.8
occ:1.00
 FE E:HEM500 0.0 29.8 1.0
ND E:HEM500 2.1 35.6 1.0
NB E:HEM500 2.1 34.8 1.0
NA E:HEM500 2.1 38.6 1.0
NC E:HEM500 2.1 32.8 1.0
SG E:CYS439 2.4 39.3 1.0
C1D E:HEM500 3.0 39.5 1.0
C4A E:HEM500 3.0 26.0 1.0
C4B E:HEM500 3.0 39.6 1.0
C1B E:HEM500 3.0 37.3 1.0
C1C E:HEM500 3.0 29.6 1.0
C4D E:HEM500 3.0 37.5 1.0
C1A E:HEM500 3.1 37.5 1.0
C4C E:HEM500 3.1 32.9 1.0
CB E:CYS439 3.3 34.1 1.0
CHB E:HEM500 3.3 31.3 1.0
CHD E:HEM500 3.3 33.3 1.0
CHC E:HEM500 3.3 34.5 1.0
CHA E:HEM500 3.4 37.9 1.0
C5 E:IND511 4.1 31.6 0.5
C2D E:HEM500 4.2 36.7 1.0
CA E:CYS439 4.2 37.6 1.0
C3A E:HEM500 4.2 39.4 1.0
C2C E:HEM500 4.2 37.5 1.0
C3D E:HEM500 4.3 35.2 1.0
C2A E:HEM500 4.3 33.7 1.0
C3B E:HEM500 4.3 38.8 1.0
C2B E:HEM500 4.3 41.4 1.0
C3C E:HEM500 4.3 39.0 1.0
C4 E:IND511 4.7 31.6 0.5
CB E:ALA301 4.8 29.1 1.0
C6 E:IND511 4.9 31.6 0.5
C6 E:IND505 4.9 31.6 0.5

Iron binding site 6 out of 6 in 2p85

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Iron binding site 6 out of 6 in the Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Structure of Human Lung Cytochrome P450 2A13 with Indole Bound in Two Alternate Conformations within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe500

b:38.6
occ:1.00
 FE F:HEM500 0.0 38.6 1.0
ND F:HEM500 2.1 32.3 1.0
NB F:HEM500 2.1 31.2 1.0
NC F:HEM500 2.1 41.0 1.0
NA F:HEM500 2.1 41.2 1.0
SG F:CYS439 2.5 52.2 1.0
C1D F:HEM500 3.0 41.1 1.0
C4B F:HEM500 3.0 42.2 1.0
C1C F:HEM500 3.0 37.8 1.0
C4D F:HEM500 3.0 43.6 1.0
C4A F:HEM500 3.1 39.4 1.0
C1B F:HEM500 3.1 41.6 1.0
C4C F:HEM500 3.1 36.5 1.0
C1A F:HEM500 3.1 40.9 1.0
CHC F:HEM500 3.3 36.1 1.0
CHB F:HEM500 3.3 42.6 1.0
CHD F:HEM500 3.3 38.3 1.0
CHA F:HEM500 3.4 44.2 1.0
C5 F:IND512 3.4 31.6 0.6
CB F:CYS439 3.5 45.0 1.0
C6 F:IND512 4.1 31.6 0.6
C2D F:HEM500 4.2 43.4 1.0
C4 F:IND512 4.2 31.6 0.6
C3D F:HEM500 4.2 42.1 1.0
C2C F:HEM500 4.2 35.3 1.0
C3A F:HEM500 4.3 46.4 1.0
C2A F:HEM500 4.3 48.1 1.0
C3C F:HEM500 4.3 44.2 1.0
C3B F:HEM500 4.3 40.2 1.0
C2B F:HEM500 4.3 36.5 1.0
CA F:CYS439 4.4 44.5 1.0
C6 F:IND506 4.5 31.6 0.4
CB F:ALA301 4.7 46.6 1.0

Reference:

B.D.Smith, J.L.Sanders, P.R.Porubsky, G.H.Lushington, C.D.Stout, E.E.Scott. Structure of the Human Lung Cytochrome P450 2A13. J.Biol.Chem. V. 282 17306 2007.
ISSN: ISSN 0021-9258
PubMed: 17428784
DOI: 10.1074/JBC.M702361200
Page generated: Sun Aug 4 01:11:05 2024

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