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Iron in PDB 5az3: Crystal Structure of Heme Binding Protein Hmut

Protein crystallography data

The structure of Crystal Structure of Heme Binding Protein Hmut, PDB code: 5az3 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) 35.45 / 1.42
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 73.040, 73.040, 147.320, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 18.2

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Heme Binding Protein Hmut (pdb code 5az3). 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, PDB code: 5az3:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5az3

Go back to Iron Binding Sites List in 5az3
Iron binding site 1 out of 2 in the Crystal Structure of Heme Binding Protein Hmut


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:9.8
occ:0.51
FE A:HEM401 0.0 9.8 0.5
FE A:HEM401 0.4 11.3 0.4
NC A:HEM401 1.8 10.4 0.4
NB A:HEM401 2.0 11.8 0.5
NC A:HEM401 2.0 11.8 0.5
ND A:HEM401 2.0 11.5 0.4
NA A:HEM401 2.1 12.8 0.5
NB A:HEM401 2.1 12.2 0.4
OH A:TYR240 2.1 12.8 1.0
NE2 A:HIS141 2.1 13.1 1.0
ND A:HEM401 2.2 13.6 0.5
NA A:HEM401 2.3 11.7 0.4
C1C A:HEM401 2.8 10.6 0.4
C4C A:HEM401 2.8 10.1 0.4
C1D A:HEM401 3.0 8.8 0.4
C4B A:HEM401 3.0 8.6 0.5
C1C A:HEM401 3.0 10.3 0.5
C4B A:HEM401 3.0 12.4 0.4
C1B A:HEM401 3.0 10.5 0.5
CZ A:TYR240 3.0 10.4 1.0
C4C A:HEM401 3.1 14.2 0.5
C4A A:HEM401 3.1 11.6 0.5
CE1 A:HIS141 3.1 12.5 1.0
C1A A:HEM401 3.1 11.9 0.5
C4D A:HEM401 3.1 9.4 0.4
CD2 A:HIS141 3.1 13.4 1.0
C1D A:HEM401 3.1 11.2 0.5
C4D A:HEM401 3.2 12.6 0.5
CHD A:HEM401 3.2 8.7 0.4
CHC A:HEM401 3.2 11.6 0.4
C1B A:HEM401 3.2 12.5 0.4
C1A A:HEM401 3.3 10.6 0.4
CHC A:HEM401 3.3 10.2 0.5
C4A A:HEM401 3.3 12.1 0.4
CHB A:HEM401 3.4 13.3 0.5
CHD A:HEM401 3.5 12.8 0.5
CHA A:HEM401 3.5 12.8 0.5
CHA A:HEM401 3.6 12.9 0.4
CHB A:HEM401 3.7 13.0 0.4
CE1 A:TYR240 3.7 11.2 1.0
CE2 A:TYR240 3.9 13.1 1.0
C2C A:HEM401 4.0 11.7 0.4
C3C A:HEM401 4.0 9.9 0.4
C3B A:HEM401 4.2 9.9 0.5
NE A:ARG242 4.2 13.1 1.0
C2B A:HEM401 4.2 11.1 0.5
ND1 A:HIS141 4.2 11.9 1.0
NH2 A:ARG242 4.2 11.4 1.0
C2C A:HEM401 4.2 14.5 0.5
C2D A:HEM401 4.2 11.6 0.4
C3C A:HEM401 4.3 14.0 0.5
CG A:HIS141 4.3 12.7 1.0
C3B A:HEM401 4.3 13.8 0.4
C3A A:HEM401 4.3 11.2 0.5
C3D A:HEM401 4.3 11.5 0.4
C2A A:HEM401 4.3 14.1 0.5
C2B A:HEM401 4.4 15.9 0.4
C2D A:HEM401 4.4 14.7 0.5
C3D A:HEM401 4.4 14.9 0.5
C2A A:HEM401 4.5 14.1 0.4
C3A A:HEM401 4.6 15.2 0.4
CZ A:ARG242 4.7 12.1 1.0
CD1 A:TYR240 4.9 12.0 1.0
CD1 A:LEU101 5.0 12.2 1.0

Iron binding site 2 out of 2 in 5az3

Go back to Iron Binding Sites List in 5az3
Iron binding site 2 out of 2 in the Crystal Structure of Heme Binding Protein Hmut


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:11.3
occ:0.44
FE A:HEM401 0.0 11.3 0.4
FE A:HEM401 0.4 9.8 0.5
ND A:HEM401 1.8 13.6 0.5
NA A:HEM401 1.9 11.7 0.4
NA A:HEM401 1.9 12.8 0.5
NB A:HEM401 2.0 12.2 0.4
ND A:HEM401 2.1 11.5 0.4
OH A:TYR240 2.1 12.8 1.0
NC A:HEM401 2.1 10.4 0.4
NE2 A:HIS141 2.2 13.1 1.0
NC A:HEM401 2.2 11.8 0.5
NB A:HEM401 2.3 11.8 0.5
C4D A:HEM401 2.8 12.6 0.5
C1A A:HEM401 2.8 11.9 0.5
C1D A:HEM401 2.9 11.2 0.5
C1A A:HEM401 2.9 10.6 0.4
C4A A:HEM401 3.0 12.1 0.4
C4D A:HEM401 3.0 9.4 0.4
C1B A:HEM401 3.0 12.5 0.4
C4A A:HEM401 3.1 11.6 0.5
C4B A:HEM401 3.1 12.4 0.4
C4C A:HEM401 3.1 14.2 0.5
CZ A:TYR240 3.1 10.4 1.0
C1C A:HEM401 3.1 10.6 0.4
C1D A:HEM401 3.1 8.8 0.4
CHA A:HEM401 3.1 12.8 0.5
CD2 A:HIS141 3.1 13.4 1.0
CE1 A:HIS141 3.2 12.5 1.0
C4C A:HEM401 3.2 10.1 0.4
C1C A:HEM401 3.3 10.3 0.5
C1B A:HEM401 3.3 10.5 0.5
CHA A:HEM401 3.3 12.9 0.4
C4B A:HEM401 3.3 8.6 0.5
CHD A:HEM401 3.4 12.8 0.5
CHB A:HEM401 3.4 13.0 0.4
CHC A:HEM401 3.5 11.6 0.4
CHD A:HEM401 3.5 8.7 0.4
CHB A:HEM401 3.6 13.3 0.5
CHC A:HEM401 3.7 10.2 0.5
CE1 A:TYR240 3.9 11.2 1.0
CE2 A:TYR240 3.9 13.1 1.0
NE A:ARG242 4.0 13.1 1.0
C3D A:HEM401 4.0 14.9 0.5
C2D A:HEM401 4.1 14.7 0.5
C2A A:HEM401 4.1 14.1 0.5
C2A A:HEM401 4.2 14.1 0.4
C3A A:HEM401 4.2 15.2 0.4
NH2 A:ARG242 4.2 11.4 1.0
C3A A:HEM401 4.2 11.2 0.5
ND1 A:HIS141 4.3 11.9 1.0
C2B A:HEM401 4.3 15.9 0.4
CG A:HIS141 4.3 12.7 1.0
C3D A:HEM401 4.3 11.5 0.4
C3B A:HEM401 4.3 13.8 0.4
C2D A:HEM401 4.3 11.6 0.4
C2C A:HEM401 4.4 11.7 0.4
C3C A:HEM401 4.4 14.0 0.5
C3C A:HEM401 4.4 9.9 0.4
C2C A:HEM401 4.5 14.5 0.5
CZ A:ARG242 4.5 12.1 1.0
C2B A:HEM401 4.5 11.1 0.5
C3B A:HEM401 4.6 9.9 0.5
CG A:ARG242 5.0 21.7 1.0
CD A:ARG242 5.0 16.6 1.0

Reference:

N.Muraki, S.Aono. Structural Basis For Heme Recognition By Hmut Responsible For Heme Transport to the Heme Transporter in Corynebacterium Glutamicum Chem Lett. 2015.
ISSN: ESSN 1348-0715
DOI: 10.1246/CL.150894
Page generated: Sun Dec 13 15:56:33 2020

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