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Iron in PDB 5b50: Crystal Structure of Heme Binding Protein Hmut Y240A

Protein crystallography data

The structure of Crystal Structure of Heme Binding Protein Hmut Y240A, PDB code: 5b50 was solved by N.Muraki, S.Aono, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.41 / 1.65
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 73.010, 73.010, 145.960, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 20.7

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Heme Binding Protein Hmut Y240A (pdb code 5b50). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Heme Binding Protein Hmut Y240A, PDB code: 5b50:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5b50

Go back to Iron Binding Sites List in 5b50
Iron binding site 1 out of 2 in the Crystal Structure of Heme Binding Protein Hmut Y240A


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 Heme Binding Protein Hmut Y240A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:17.9
occ:0.42
FE A:HEM401 0.0 17.9 0.4
FE A:HEM401 0.3 22.1 0.6
NC A:HEM401 1.8 18.7 0.6
NC A:HEM401 1.9 20.0 0.4
ND A:HEM401 2.0 15.4 0.6
NB A:HEM401 2.0 18.4 0.4
ND A:HEM401 2.1 20.1 0.4
NB A:HEM401 2.1 20.7 0.6
NA A:HEM401 2.1 16.1 0.4
NE2 A:HIS141 2.2 18.8 1.0
O A:HOH542 2.3 28.1 1.0
NA A:HEM401 2.3 19.6 0.6
C1C A:HEM401 2.8 20.9 0.6
C4C A:HEM401 2.8 19.2 0.6
C1D A:HEM401 2.9 16.6 0.6
C4C A:HEM401 3.0 24.6 0.4
C1C A:HEM401 3.0 22.2 0.4
C4B A:HEM401 3.0 19.6 0.4
C4B A:HEM401 3.0 24.1 0.6
C1D A:HEM401 3.0 22.0 0.4
C1B A:HEM401 3.1 18.0 0.4
C4D A:HEM401 3.1 17.6 0.6
C4D A:HEM401 3.1 21.1 0.4
C4A A:HEM401 3.1 18.2 0.4
C1A A:HEM401 3.2 21.6 0.4
CD2 A:HIS141 3.2 23.9 1.0
CE1 A:HIS141 3.2 22.4 1.0
CHC A:HEM401 3.2 22.9 0.6
C1B A:HEM401 3.2 24.4 0.6
CHD A:HEM401 3.3 17.3 0.6
C1A A:HEM401 3.3 21.8 0.6
CHC A:HEM401 3.3 20.9 0.4
C4A A:HEM401 3.3 21.3 0.6
CHD A:HEM401 3.3 24.9 0.4
CHB A:HEM401 3.5 15.7 0.4
CHA A:HEM401 3.5 21.8 0.4
CHA A:HEM401 3.6 21.3 0.6
CHB A:HEM401 3.7 21.2 0.6
C2C A:HEM401 4.0 23.4 0.6
C3C A:HEM401 4.0 21.0 0.6
NE A:ARG242 4.2 22.7 1.0
C3C A:HEM401 4.2 27.9 0.4
C2C A:HEM401 4.2 25.9 0.4
C2D A:HEM401 4.2 18.6 0.6
C3B A:HEM401 4.2 18.0 0.4
O A:HOH634 4.3 25.5 1.0
C3D A:HEM401 4.3 19.1 0.6
C2B A:HEM401 4.3 14.9 0.4
C2D A:HEM401 4.3 24.0 0.4
ND1 A:HIS141 4.3 16.4 1.0
NH2 A:ARG242 4.3 24.2 1.0
CG A:HIS141 4.3 17.9 1.0
C3B A:HEM401 4.3 28.7 0.6
C3D A:HEM401 4.3 23.2 0.4
C3A A:HEM401 4.4 19.4 0.4
C2A A:HEM401 4.4 25.2 0.4
C2B A:HEM401 4.4 29.5 0.6
C3A A:HEM401 4.6 22.4 0.6
C2A A:HEM401 4.6 22.4 0.6
CZ A:ARG242 4.6 25.8 1.0
CD1 A:LEU101 4.9 16.0 1.0

Iron binding site 2 out of 2 in 5b50

Go back to Iron Binding Sites List in 5b50
Iron binding site 2 out of 2 in the Crystal Structure of Heme Binding Protein Hmut Y240A


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 Heme Binding Protein Hmut Y240A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:22.1
occ:0.58
FE A:HEM401 0.0 22.1 0.6
FE A:HEM401 0.3 17.9 0.4
ND A:HEM401 1.8 20.1 0.4
NA A:HEM401 1.9 16.1 0.4
ND A:HEM401 2.0 15.4 0.6
NA A:HEM401 2.0 19.6 0.6
NC A:HEM401 2.1 18.7 0.6
NB A:HEM401 2.1 20.7 0.6
NE2 A:HIS141 2.1 18.8 1.0
NC A:HEM401 2.2 20.0 0.4
NB A:HEM401 2.3 18.4 0.4
O A:HOH542 2.4 28.1 1.0
C4D A:HEM401 2.8 21.1 0.4
C1D A:HEM401 2.9 22.0 0.4
C1A A:HEM401 2.9 21.6 0.4
C4D A:HEM401 2.9 17.6 0.6
C1A A:HEM401 3.0 21.8 0.6
C1D A:HEM401 3.0 16.6 0.6
C4A A:HEM401 3.0 21.3 0.6
C4C A:HEM401 3.1 24.6 0.4
C4A A:HEM401 3.1 18.2 0.4
CD2 A:HIS141 3.1 23.9 1.0
C1C A:HEM401 3.1 20.9 0.6
CE1 A:HIS141 3.1 22.4 1.0
C4C A:HEM401 3.1 19.2 0.6
C1B A:HEM401 3.1 24.4 0.6
C4B A:HEM401 3.1 24.1 0.6
CHA A:HEM401 3.2 21.8 0.4
C1C A:HEM401 3.3 22.2 0.4
C1B A:HEM401 3.3 18.0 0.4
CHD A:HEM401 3.3 24.9 0.4
C4B A:HEM401 3.3 19.6 0.4
CHA A:HEM401 3.3 21.3 0.6
CHB A:HEM401 3.5 21.2 0.6
CHD A:HEM401 3.5 17.3 0.6
CHC A:HEM401 3.5 22.9 0.6
CHB A:HEM401 3.5 15.7 0.4
CHC A:HEM401 3.7 20.9 0.4
C3D A:HEM401 4.0 23.2 0.4
C2D A:HEM401 4.0 24.0 0.4
NE A:ARG242 4.1 22.7 1.0
C2A A:HEM401 4.2 25.2 0.4
C3D A:HEM401 4.2 19.1 0.6
C3A A:HEM401 4.2 19.4 0.4
C2D A:HEM401 4.2 18.6 0.6
ND1 A:HIS141 4.2 16.4 1.0
C2A A:HEM401 4.2 22.4 0.6
C3A A:HEM401 4.2 22.4 0.6
CG A:HIS141 4.2 17.9 1.0
NH2 A:ARG242 4.3 24.2 1.0
C2C A:HEM401 4.3 23.4 0.6
C3C A:HEM401 4.3 27.9 0.4
C3C A:HEM401 4.4 21.0 0.6
C2B A:HEM401 4.4 29.5 0.6
C3B A:HEM401 4.4 28.7 0.6
O A:HOH634 4.4 25.5 1.0
C2C A:HEM401 4.4 25.9 0.4
C2B A:HEM401 4.5 14.9 0.4
C3B A:HEM401 4.5 18.0 0.4
CZ A:ARG242 4.6 25.8 1.0
CG A:ARG242 4.9 28.1 1.0
CD A:ARG242 5.0 27.7 1.0

Reference:

N.Muraki, C.Kitatsuji, M.Ogura, T.Uchida, K.Ishimori, S.Aono. Structural Characterization of Heme Environmental Mutants of Cghmut That Shuttles Heme Molecules to Heme Transporters Int J Mol Sci V. 17 2016.
ISSN: ESSN 1422-0067
PubMed: 27240352
DOI: 10.3390/IJMS17060829
Page generated: Sun Dec 13 15:56:51 2020

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