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Iron in PDB 1mdv: Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies

Protein crystallography data

The structure of Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies, PDB code: 1mdv was solved by A.Dolla, P.Arnoux, I.Protasevich, V.Lobachov, M.Brugna, M.T.Guidici-Orticoni, R.Haser, M.Czjzek, A.Makarov, M.Brushi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.30
Space group P 4
Cell size a, b, c (Å), α, β, γ (°) 97.220, 97.220, 36.030, 90.00, 90.00, 90.00
R / Rfree (%) 22.4 / 29.6

Iron Binding Sites:

The binding sites of Iron atom in the Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies (pdb code 1mdv). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies, PDB code: 1mdv:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in 1mdv

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Iron binding site 1 out of 8 in the Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe110

b:26.2
occ:1.00
FE A:HEM110 0.0 26.2 1.0
NA A:HEM110 2.0 35.6 1.0
NB A:HEM110 2.0 31.9 1.0
ND A:HEM110 2.0 32.3 1.0
NC A:HEM110 2.0 28.2 1.0
NE2 A:HIS34 2.0 21.6 1.0
NE2 A:HIS22 2.0 22.6 1.0
CE1 A:HIS22 2.9 24.0 1.0
CE1 A:HIS34 2.9 24.4 1.0
C1A A:HEM110 3.0 36.3 1.0
C4B A:HEM110 3.0 32.7 1.0
C1C A:HEM110 3.0 30.1 1.0
C4D A:HEM110 3.0 33.3 1.0
C1B A:HEM110 3.0 35.3 1.0
C4A A:HEM110 3.0 35.8 1.0
C4C A:HEM110 3.0 26.5 1.0
C1D A:HEM110 3.0 30.7 1.0
CD2 A:HIS34 3.1 26.9 1.0
CD2 A:HIS22 3.2 24.6 1.0
CHC A:HEM110 3.4 28.3 1.0
CHA A:HEM110 3.4 33.6 1.0
CHB A:HEM110 3.4 35.2 1.0
CHD A:HEM110 3.4 29.3 1.0
ND1 A:HIS22 4.1 22.2 1.0
ND1 A:HIS34 4.1 22.7 1.0
CG A:HIS34 4.2 24.5 1.0
C2A A:HEM110 4.2 37.6 1.0
C3D A:HEM110 4.2 33.8 1.0
CG A:HIS22 4.3 21.9 1.0
C3A A:HEM110 4.3 35.4 1.0
C2B A:HEM110 4.3 34.2 1.0
C3B A:HEM110 4.3 33.3 1.0
C2C A:HEM110 4.3 29.2 1.0
C2D A:HEM110 4.3 30.7 1.0
C3C A:HEM110 4.3 26.8 1.0
CD2 A:LEU20 5.0 28.8 1.0

Iron binding site 2 out of 8 in 1mdv

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Iron binding site 2 out of 8 in the Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe111

b:38.6
occ:1.00
FE A:HEM111 0.0 38.6 1.0
NC A:HEM111 2.0 39.9 1.0
ND A:HEM111 2.0 39.6 1.0
NA A:HEM111 2.0 32.3 1.0
NB A:HEM111 2.0 35.0 1.0
NE2 A:HIS52 2.0 38.8 1.0
NE2 A:HIS35 2.0 38.4 1.0
CE1 A:HIS52 3.0 39.1 1.0
CE1 A:HIS35 3.0 38.4 1.0
C1C A:HEM111 3.0 39.3 1.0
C4C A:HEM111 3.0 40.9 1.0
C1D A:HEM111 3.0 42.1 1.0
C4D A:HEM111 3.0 40.6 1.0
C4B A:HEM111 3.0 34.3 1.0
C1A A:HEM111 3.1 32.6 1.0
C4A A:HEM111 3.1 29.2 1.0
C1B A:HEM111 3.1 31.3 1.0
CD2 A:HIS35 3.1 40.6 1.0
CD2 A:HIS52 3.2 39.0 1.0
CHC A:HEM111 3.4 37.9 1.0
CHD A:HEM111 3.4 40.9 1.0
CHA A:HEM111 3.4 36.0 1.0
CHB A:HEM111 3.4 28.9 1.0
ND1 A:HIS52 4.2 39.1 1.0
ND1 A:HIS35 4.2 41.0 1.0
C2C A:HEM111 4.3 38.4 1.0
C2D A:HEM111 4.3 43.3 1.0
CG A:HIS35 4.3 43.1 1.0
C3C A:HEM111 4.3 39.9 1.0
C3D A:HEM111 4.3 42.8 1.0
CG A:HIS52 4.3 40.7 1.0
C3A A:HEM111 4.3 29.4 1.0
C2A A:HEM111 4.3 30.2 1.0
C3B A:HEM111 4.3 30.7 1.0
C2B A:HEM111 4.3 30.8 1.0

Iron binding site 3 out of 8 in 1mdv

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Iron binding site 3 out of 8 in the Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe112

b:19.0
occ:1.00
FE A:HEM112 0.0 19.0 1.0
NC A:HEM112 1.9 11.0 1.0
NA A:HEM112 2.0 16.2 1.0
ND A:HEM112 2.0 17.5 1.0
NB A:HEM112 2.0 18.0 1.0
NE2 A:HIS25 2.0 16.9 1.0
NE2 A:HIS83 2.1 17.8 1.0
CE1 A:HIS83 3.0 15.2 1.0
C4C A:HEM112 3.0 19.3 1.0
CE1 A:HIS25 3.0 18.5 1.0
C1C A:HEM112 3.0 16.4 1.0
C1A A:HEM112 3.0 22.2 1.0
C1D A:HEM112 3.0 16.2 1.0
C4D A:HEM112 3.0 18.8 1.0
C4A A:HEM112 3.0 20.2 1.0
C4B A:HEM112 3.1 16.0 1.0
C1B A:HEM112 3.1 16.6 1.0
CD2 A:HIS25 3.1 17.3 1.0
CD2 A:HIS83 3.2 16.9 1.0
CHD A:HEM112 3.4 15.9 1.0
CHA A:HEM112 3.4 16.6 1.0
CHC A:HEM112 3.4 17.7 1.0
CHB A:HEM112 3.5 18.0 1.0
ND1 A:HIS25 4.2 17.6 1.0
ND1 A:HIS83 4.2 14.1 1.0
C2A A:HEM112 4.2 23.6 1.0
C3C A:HEM112 4.2 18.0 1.0
C2C A:HEM112 4.2 13.4 1.0
C2D A:HEM112 4.2 17.5 1.0
CG A:HIS25 4.3 20.6 1.0
C3D A:HEM112 4.3 19.4 1.0
C3A A:HEM112 4.3 18.5 1.0
CG A:HIS83 4.3 14.8 1.0
C2B A:HEM112 4.4 17.8 1.0
C3B A:HEM112 4.4 19.2 1.0

Iron binding site 4 out of 8 in 1mdv

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Iron binding site 4 out of 8 in the Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe113

b:17.9
occ:1.00
FE A:HEM113 0.0 17.9 1.0
NE2 A:HIS106 1.9 11.8 1.0
NB A:HEM113 2.0 26.6 1.0
NE2 A:HIS70 2.0 13.9 1.0
NA A:HEM113 2.0 28.6 1.0
NC A:HEM113 2.0 26.5 1.0
ND A:HEM113 2.0 22.8 1.0
CE1 A:HIS106 2.9 14.5 1.0
CE1 A:HIS70 2.9 16.5 1.0
C1B A:HEM113 3.0 31.1 1.0
C4A A:HEM113 3.0 27.9 1.0
C4B A:HEM113 3.0 30.5 1.0
C1C A:HEM113 3.1 24.9 1.0
C1D A:HEM113 3.1 25.4 1.0
C4C A:HEM113 3.1 28.5 1.0
CD2 A:HIS106 3.1 16.3 1.0
C4D A:HEM113 3.1 24.5 1.0
C1A A:HEM113 3.1 24.7 1.0
CD2 A:HIS70 3.1 16.5 1.0
CHB A:HEM113 3.4 28.0 1.0
CHC A:HEM113 3.4 28.7 1.0
CHD A:HEM113 3.4 27.1 1.0
CHA A:HEM113 3.5 23.1 1.0
ND1 A:HIS106 4.0 14.4 1.0
ND1 A:HIS70 4.1 13.7 1.0
CG A:HIS106 4.2 14.3 1.0
CG A:HIS70 4.2 16.2 1.0
C2B A:HEM113 4.3 32.5 1.0
C3A A:HEM113 4.3 28.5 1.0
C3B A:HEM113 4.3 29.2 1.0
C2C A:HEM113 4.3 25.1 1.0
C2A A:HEM113 4.3 29.6 1.0
C2D A:HEM113 4.3 26.1 1.0
C3D A:HEM113 4.3 26.6 1.0
C3C A:HEM113 4.3 25.5 1.0

Iron binding site 5 out of 8 in 1mdv

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Iron binding site 5 out of 8 in the Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe110

b:24.9
occ:1.00
FE B:HEM110 0.0 24.9 1.0
NA B:HEM110 2.0 29.2 1.0
NE2 B:HIS34 2.0 20.2 1.0
ND B:HEM110 2.0 34.9 1.0
NC B:HEM110 2.0 28.7 1.0
NB B:HEM110 2.0 32.6 1.0
NE2 B:HIS22 2.0 22.5 1.0
CE1 B:HIS34 2.9 20.3 1.0
C1A B:HEM110 3.0 33.2 1.0
C4D B:HEM110 3.0 33.7 1.0
C4A B:HEM110 3.0 34.2 1.0
C4C B:HEM110 3.0 30.3 1.0
CE1 B:HIS22 3.0 25.5 1.0
C1D B:HEM110 3.0 32.6 1.0
C1C B:HEM110 3.1 33.4 1.0
CD2 B:HIS22 3.1 23.8 1.0
C1B B:HEM110 3.1 34.9 1.0
C4B B:HEM110 3.1 34.0 1.0
CD2 B:HIS34 3.1 22.8 1.0
CHA B:HEM110 3.4 34.2 1.0
CHD B:HEM110 3.4 31.5 1.0
CHB B:HEM110 3.4 33.7 1.0
CHC B:HEM110 3.4 33.7 1.0
ND1 B:HIS34 4.1 17.9 1.0
ND1 B:HIS22 4.2 22.3 1.0
CG B:HIS34 4.2 19.7 1.0
CG B:HIS22 4.2 24.4 1.0
C2A B:HEM110 4.3 34.2 1.0
C3D B:HEM110 4.3 36.9 1.0
C3A B:HEM110 4.3 33.8 1.0
C2D B:HEM110 4.3 33.0 1.0
C2C B:HEM110 4.3 33.1 1.0
C3C B:HEM110 4.3 30.4 1.0
C2B B:HEM110 4.3 34.8 1.0
C3B B:HEM110 4.4 33.5 1.0

Iron binding site 6 out of 8 in 1mdv

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Iron binding site 6 out of 8 in the Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe111

b:34.7
occ:1.00
FE B:HEM111 0.0 34.7 1.0
ND B:HEM111 1.9 35.0 1.0
NC B:HEM111 2.0 34.0 1.0
NA B:HEM111 2.0 29.7 1.0
NB B:HEM111 2.0 31.6 1.0
NE2 B:HIS35 2.0 38.9 1.0
NE2 B:HIS52 2.0 34.2 1.0
CE1 B:HIS52 3.0 33.0 1.0
CE1 B:HIS35 3.0 41.0 1.0
C1D B:HEM111 3.0 38.2 1.0
C4D B:HEM111 3.0 38.2 1.0
C4C B:HEM111 3.0 36.5 1.0
C1C B:HEM111 3.0 34.7 1.0
C1A B:HEM111 3.0 34.0 1.0
C4A B:HEM111 3.0 30.5 1.0
C1B B:HEM111 3.1 29.1 1.0
C4B B:HEM111 3.1 29.4 1.0
CD2 B:HIS35 3.1 38.8 1.0
CD2 B:HIS52 3.1 32.5 1.0
CHA B:HEM111 3.4 35.4 1.0
CHD B:HEM111 3.4 37.1 1.0
CHC B:HEM111 3.4 33.8 1.0
CHB B:HEM111 3.4 29.1 1.0
ND1 B:HIS52 4.1 32.8 1.0
ND1 B:HIS35 4.2 41.5 1.0
CG B:HIS35 4.2 42.5 1.0
C3D B:HEM111 4.2 40.7 1.0
C2D B:HEM111 4.2 38.0 1.0
CG B:HIS52 4.3 32.6 1.0
C2A B:HEM111 4.3 33.9 1.0
C2C B:HEM111 4.3 39.0 1.0
C3C B:HEM111 4.3 39.1 1.0
C3A B:HEM111 4.3 31.4 1.0
C2B B:HEM111 4.3 28.8 1.0
C3B B:HEM111 4.3 27.2 1.0

Iron binding site 7 out of 8 in 1mdv

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Iron binding site 7 out of 8 in the Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe112

b:33.0
occ:1.00
FE B:HEM112 0.0 33.0 1.0
NA B:HEM112 2.0 27.8 1.0
ND B:HEM112 2.0 34.5 1.0
NB B:HEM112 2.0 26.5 1.0
NC B:HEM112 2.0 25.7 1.0
NE2 B:HIS25 2.1 33.2 1.0
NE2 B:HIS83 2.1 33.5 1.0
C1A B:HEM112 3.0 35.2 1.0
C4D B:HEM112 3.0 36.6 1.0
C4B B:HEM112 3.0 25.6 1.0
CE1 B:HIS83 3.0 31.3 1.0
C1C B:HEM112 3.0 27.9 1.0
C1B B:HEM112 3.0 26.4 1.0
C4A B:HEM112 3.0 28.8 1.0
C1D B:HEM112 3.0 32.6 1.0
C4C B:HEM112 3.1 27.6 1.0
CE1 B:HIS25 3.1 31.4 1.0
CD2 B:HIS25 3.1 32.8 1.0
CD2 B:HIS83 3.2 33.2 1.0
CHA B:HEM112 3.4 35.4 1.0
CHC B:HEM112 3.4 26.2 1.0
CHB B:HEM112 3.4 26.4 1.0
CHD B:HEM112 3.4 31.1 1.0
ND1 B:HIS83 4.2 30.6 1.0
ND1 B:HIS25 4.2 29.3 1.0
C2A B:HEM112 4.3 34.2 1.0
CG B:HIS25 4.3 37.5 1.0
C3D B:HEM112 4.3 39.0 1.0
C2D B:HEM112 4.3 36.6 1.0
C3A B:HEM112 4.3 27.6 1.0
C2B B:HEM112 4.3 26.3 1.0
C2C B:HEM112 4.3 25.2 1.0
C3B B:HEM112 4.3 26.8 1.0
CG B:HIS83 4.3 32.9 1.0
C3C B:HEM112 4.3 26.3 1.0

Iron binding site 8 out of 8 in 1mdv

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Iron binding site 8 out of 8 in the Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability and Function Studies within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe113

b:27.6
occ:1.00
FE B:HEM113 0.0 27.6 1.0
NE2 B:HIS106 2.0 25.2 1.0
ND B:HEM113 2.0 30.6 1.0
NA B:HEM113 2.0 34.4 1.0
NC B:HEM113 2.0 31.1 1.0
NB B:HEM113 2.0 33.5 1.0
NE2 B:HIS70 2.0 16.6 1.0
CE1 B:HIS106 2.8 27.5 1.0
CE1 B:HIS70 3.0 12.6 1.0
C1D B:HEM113 3.0 30.9 1.0
C4A B:HEM113 3.0 36.7 1.0
C4D B:HEM113 3.1 33.6 1.0
C1B B:HEM113 3.1 35.9 1.0
C1C B:HEM113 3.1 31.6 1.0
C1A B:HEM113 3.1 36.4 1.0
C4C B:HEM113 3.1 30.1 1.0
C4B B:HEM113 3.1 37.4 1.0
CD2 B:HIS70 3.1 15.1 1.0
CD2 B:HIS106 3.1 29.5 1.0
CHD B:HEM113 3.4 30.5 1.0
CHB B:HEM113 3.4 36.8 1.0
CHC B:HEM113 3.4 35.7 1.0
CHA B:HEM113 3.4 34.4 1.0
ND1 B:HIS106 4.0 30.5 1.0
ND1 B:HIS70 4.1 14.0 1.0
CG B:HIS106 4.2 30.5 1.0
CG B:HIS70 4.3 13.4 1.0
C2D B:HEM113 4.3 31.6 1.0
C3A B:HEM113 4.3 38.6 1.0
C3D B:HEM113 4.3 32.6 1.0
C2B B:HEM113 4.3 36.4 1.0
C2C B:HEM113 4.3 29.6 1.0
C2A B:HEM113 4.3 39.9 1.0
C3C B:HEM113 4.4 30.2 1.0
C3B B:HEM113 4.4 37.6 1.0

Reference:

A.Dolla, P.Arnoux, I.Protasevich, V.Lobachov, M.Brugna, M.T.Giudici-Orticoni, R.Haser, M.Czjzek, A.Makarov, M.Bruschi. Key Role of Phenylalanine 20 in Cytochrome C3: Structure, Stability, and Function Studies. Biochemistry V. 38 33 1999.
ISSN: ISSN 0006-2960
PubMed: 9890880
DOI: 10.1021/BI981593H
Page generated: Wed Jul 16 18:02:15 2025

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