Iron in PDB 1hco: The Structure of Human Carbonmonoxy Haemoglobin at 2.7 Angstroms Resolution
Protein crystallography data
The structure of The Structure of Human Carbonmonoxy Haemoglobin at 2.7 Angstroms Resolution, PDB code: 1hco
was solved by
J.M.Baldwin,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
N/A /
2.70
|
Space group
|
P 41 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
53.700,
53.700,
193.000,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
n/a /
n/a
|
Iron Binding Sites:
The binding sites of Iron atom in the The Structure of Human Carbonmonoxy Haemoglobin at 2.7 Angstroms Resolution
(pdb code 1hco). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
The Structure of Human Carbonmonoxy Haemoglobin at 2.7 Angstroms Resolution, PDB code: 1hco:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 1hco
Go back to
Iron Binding Sites List in 1hco
Iron binding site 1 out
of 2 in the The Structure of Human Carbonmonoxy Haemoglobin at 2.7 Angstroms Resolution
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of The Structure of Human Carbonmonoxy Haemoglobin at 2.7 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe200
b:0.0
occ:1.00
|
FE
|
A:HEM200
|
0.0
|
0.0
|
1.0
|
C
|
A:CMO201
|
1.8
|
0.0
|
1.0
|
NB
|
A:HEM200
|
2.0
|
0.0
|
1.0
|
NC
|
A:HEM200
|
2.0
|
0.0
|
1.0
|
ND
|
A:HEM200
|
2.0
|
0.0
|
1.0
|
NA
|
A:HEM200
|
2.0
|
0.0
|
1.0
|
NE2
|
A:HIS87
|
2.1
|
0.0
|
1.0
|
CE1
|
A:HIS87
|
2.7
|
0.0
|
1.0
|
C1A
|
A:HEM200
|
3.0
|
0.0
|
1.0
|
C4D
|
A:HEM200
|
3.0
|
0.0
|
1.0
|
C1D
|
A:HEM200
|
3.0
|
0.0
|
1.0
|
C1C
|
A:HEM200
|
3.0
|
0.0
|
1.0
|
C4A
|
A:HEM200
|
3.0
|
0.0
|
1.0
|
C1B
|
A:HEM200
|
3.0
|
0.0
|
1.0
|
C4B
|
A:HEM200
|
3.0
|
0.0
|
1.0
|
C4C
|
A:HEM200
|
3.0
|
0.0
|
1.0
|
O
|
A:CMO201
|
3.1
|
0.0
|
1.0
|
CD2
|
A:HIS87
|
3.2
|
0.0
|
1.0
|
CHD
|
A:HEM200
|
3.4
|
0.0
|
1.0
|
CHC
|
A:HEM200
|
3.4
|
0.0
|
1.0
|
CHB
|
A:HEM200
|
3.4
|
0.0
|
1.0
|
CHA
|
A:HEM200
|
3.4
|
0.0
|
1.0
|
ND1
|
A:HIS87
|
4.0
|
0.0
|
1.0
|
CG
|
A:HIS87
|
4.2
|
0.0
|
1.0
|
C3C
|
A:HEM200
|
4.3
|
0.0
|
1.0
|
C3B
|
A:HEM200
|
4.3
|
0.0
|
1.0
|
C2C
|
A:HEM200
|
4.3
|
0.0
|
1.0
|
C2B
|
A:HEM200
|
4.3
|
0.0
|
1.0
|
C3D
|
A:HEM200
|
4.3
|
0.0
|
1.0
|
C2D
|
A:HEM200
|
4.3
|
0.0
|
1.0
|
C3A
|
A:HEM200
|
4.3
|
0.0
|
1.0
|
C2A
|
A:HEM200
|
4.3
|
0.0
|
1.0
|
CG2
|
A:VAL62
|
4.9
|
0.0
|
1.0
|
NE2
|
A:HIS58
|
4.9
|
0.0
|
1.0
|
|
Iron binding site 2 out
of 2 in 1hco
Go back to
Iron Binding Sites List in 1hco
Iron binding site 2 out
of 2 in the The Structure of Human Carbonmonoxy Haemoglobin at 2.7 Angstroms Resolution
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of The Structure of Human Carbonmonoxy Haemoglobin at 2.7 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe200
b:0.0
occ:1.00
|
FE
|
B:HEM200
|
0.0
|
0.0
|
1.0
|
C
|
B:CMO201
|
1.8
|
0.0
|
1.0
|
NE2
|
B:HIS92
|
1.8
|
0.0
|
1.0
|
NC
|
B:HEM200
|
2.0
|
0.0
|
1.0
|
ND
|
B:HEM200
|
2.0
|
0.0
|
1.0
|
NB
|
B:HEM200
|
2.0
|
0.0
|
1.0
|
NA
|
B:HEM200
|
2.0
|
0.0
|
1.0
|
CD2
|
B:HIS92
|
2.8
|
0.0
|
1.0
|
CE1
|
B:HIS92
|
2.8
|
0.0
|
1.0
|
C1C
|
B:HEM200
|
3.0
|
0.0
|
1.0
|
C1D
|
B:HEM200
|
3.0
|
0.0
|
1.0
|
C4C
|
B:HEM200
|
3.0
|
0.0
|
1.0
|
C4B
|
B:HEM200
|
3.0
|
0.0
|
1.0
|
C4D
|
B:HEM200
|
3.0
|
0.0
|
1.0
|
C4A
|
B:HEM200
|
3.0
|
0.0
|
1.0
|
C1B
|
B:HEM200
|
3.1
|
0.0
|
1.0
|
C1A
|
B:HEM200
|
3.1
|
0.0
|
1.0
|
O
|
B:CMO201
|
3.1
|
0.0
|
1.0
|
CHC
|
B:HEM200
|
3.4
|
0.0
|
1.0
|
CHD
|
B:HEM200
|
3.4
|
0.0
|
1.0
|
CHA
|
B:HEM200
|
3.4
|
0.0
|
1.0
|
CHB
|
B:HEM200
|
3.4
|
0.0
|
1.0
|
ND1
|
B:HIS92
|
3.9
|
0.0
|
1.0
|
CG
|
B:HIS92
|
3.9
|
0.0
|
1.0
|
C2C
|
B:HEM200
|
4.3
|
0.0
|
1.0
|
C3C
|
B:HEM200
|
4.3
|
0.0
|
1.0
|
C3B
|
B:HEM200
|
4.3
|
0.0
|
1.0
|
C2B
|
B:HEM200
|
4.3
|
0.0
|
1.0
|
C2D
|
B:HEM200
|
4.3
|
0.0
|
1.0
|
C3D
|
B:HEM200
|
4.3
|
0.0
|
1.0
|
C2A
|
B:HEM200
|
4.3
|
0.0
|
1.0
|
C3A
|
B:HEM200
|
4.3
|
0.0
|
1.0
|
NE2
|
B:HIS63
|
4.4
|
0.0
|
1.0
|
|
Reference:
J.M.Baldwin,
J.M.Baldwin.
N/A N/A.
ISSN: ISSN 0022-2836
PubMed: 7373648
DOI: 10.1016/0022-2836(80)90308-3
Page generated: Sat Aug 3 07:24:56 2024
|