Iron in PDB 9hek: Trimeric CD163 Bound to Human Haptoglobin-Haemoglobin Complex
Other elements in 9hek:
The structure of Trimeric CD163 Bound to Human Haptoglobin-Haemoglobin Complex also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Trimeric CD163 Bound to Human Haptoglobin-Haemoglobin Complex
(pdb code 9hek). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
Trimeric CD163 Bound to Human Haptoglobin-Haemoglobin Complex, PDB code: 9hek:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 9hek
Go back to
Iron Binding Sites List in 9hek
Iron binding site 1 out
of 2 in the Trimeric CD163 Bound to Human Haptoglobin-Haemoglobin Complex
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Trimeric CD163 Bound to Human Haptoglobin-Haemoglobin Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe201
b:87.8
occ:1.00
|
FE
|
D:HEM201
|
0.0
|
87.8
|
1.0
|
NA
|
D:HEM201
|
2.0
|
73.8
|
1.0
|
NB
|
D:HEM201
|
2.0
|
75.1
|
1.0
|
ND
|
D:HEM201
|
2.0
|
89.6
|
1.0
|
NC
|
D:HEM201
|
2.0
|
76.0
|
1.0
|
NE2
|
D:HIS88
|
2.2
|
67.4
|
1.0
|
CE1
|
D:HIS88
|
2.7
|
60.3
|
1.0
|
C4A
|
D:HEM201
|
3.0
|
70.4
|
1.0
|
C1B
|
D:HEM201
|
3.1
|
73.7
|
1.0
|
C1A
|
D:HEM201
|
3.1
|
79.1
|
1.0
|
C4C
|
D:HEM201
|
3.1
|
75.0
|
1.0
|
C1D
|
D:HEM201
|
3.1
|
88.7
|
1.0
|
C4B
|
D:HEM201
|
3.1
|
72.5
|
1.0
|
C1C
|
D:HEM201
|
3.1
|
76.6
|
1.0
|
C4D
|
D:HEM201
|
3.1
|
89.1
|
1.0
|
CHB
|
D:HEM201
|
3.4
|
72.8
|
1.0
|
CHC
|
D:HEM201
|
3.4
|
75.2
|
1.0
|
CHA
|
D:HEM201
|
3.4
|
86.7
|
1.0
|
CHD
|
D:HEM201
|
3.4
|
85.8
|
1.0
|
CD2
|
D:HIS88
|
3.4
|
63.2
|
1.0
|
O2
|
D:OXY202
|
3.6
|
85.3
|
1.0
|
ND1
|
D:HIS88
|
3.9
|
53.8
|
1.0
|
CE1
|
D:HIS59
|
4.1
|
94.4
|
1.0
|
O1
|
D:OXY202
|
4.2
|
91.4
|
1.0
|
C3A
|
D:HEM201
|
4.3
|
73.6
|
1.0
|
C2A
|
D:HEM201
|
4.3
|
76.0
|
1.0
|
C2B
|
D:HEM201
|
4.3
|
69.3
|
1.0
|
C2D
|
D:HEM201
|
4.3
|
88.2
|
1.0
|
C3B
|
D:HEM201
|
4.3
|
66.9
|
1.0
|
C3D
|
D:HEM201
|
4.3
|
90.6
|
1.0
|
C2C
|
D:HEM201
|
4.3
|
72.4
|
1.0
|
C3C
|
D:HEM201
|
4.3
|
70.5
|
1.0
|
CG
|
D:HIS88
|
4.3
|
51.0
|
1.0
|
CG2
|
D:VAL63
|
4.6
|
74.8
|
1.0
|
NE2
|
D:HIS59
|
4.6
|
97.2
|
1.0
|
|
Iron binding site 2 out
of 2 in 9hek
Go back to
Iron Binding Sites List in 9hek
Iron binding site 2 out
of 2 in the Trimeric CD163 Bound to Human Haptoglobin-Haemoglobin Complex
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Trimeric CD163 Bound to Human Haptoglobin-Haemoglobin Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe201
b:102.7
occ:1.00
|
FE
|
E:HEM201
|
0.0
|
102.7
|
1.0
|
NC
|
E:HEM201
|
2.0
|
110.0
|
1.0
|
NA
|
E:HEM201
|
2.1
|
116.6
|
1.0
|
ND
|
E:HEM201
|
2.1
|
100.2
|
1.0
|
NB
|
E:HEM201
|
2.1
|
104.3
|
1.0
|
NE2
|
E:HIS93
|
2.3
|
94.2
|
1.0
|
CE1
|
E:HIS93
|
2.8
|
96.7
|
1.0
|
C1C
|
E:HEM201
|
3.0
|
105.7
|
1.0
|
C4D
|
E:HEM201
|
3.1
|
101.8
|
1.0
|
C1A
|
E:HEM201
|
3.1
|
113.9
|
1.0
|
C4B
|
E:HEM201
|
3.1
|
105.0
|
1.0
|
C4C
|
E:HEM201
|
3.1
|
107.5
|
1.0
|
C4A
|
E:HEM201
|
3.1
|
116.0
|
1.0
|
C1B
|
E:HEM201
|
3.1
|
107.5
|
1.0
|
C1D
|
E:HEM201
|
3.1
|
100.7
|
1.0
|
O1
|
E:OXY202
|
3.4
|
108.4
|
1.0
|
CHC
|
E:HEM201
|
3.4
|
104.5
|
1.0
|
CHA
|
E:HEM201
|
3.4
|
106.3
|
1.0
|
CHB
|
E:HEM201
|
3.4
|
109.0
|
1.0
|
CHD
|
E:HEM201
|
3.4
|
104.1
|
1.0
|
CD2
|
E:HIS93
|
3.5
|
92.0
|
1.0
|
CE1
|
E:HIS64
|
4.1
|
104.1
|
1.0
|
ND1
|
E:HIS93
|
4.1
|
96.8
|
1.0
|
C2C
|
E:HEM201
|
4.3
|
96.1
|
1.0
|
C2B
|
E:HEM201
|
4.3
|
108.9
|
1.0
|
C3D
|
E:HEM201
|
4.3
|
103.1
|
1.0
|
C3C
|
E:HEM201
|
4.3
|
99.2
|
1.0
|
C3A
|
E:HEM201
|
4.3
|
119.0
|
1.0
|
C2A
|
E:HEM201
|
4.3
|
120.1
|
1.0
|
C3B
|
E:HEM201
|
4.3
|
109.0
|
1.0
|
C2D
|
E:HEM201
|
4.3
|
100.5
|
1.0
|
O2
|
E:OXY202
|
4.3
|
107.4
|
1.0
|
CG
|
E:HIS93
|
4.4
|
92.0
|
1.0
|
CG1
|
E:VAL68
|
4.5
|
93.0
|
1.0
|
NE2
|
E:HIS64
|
4.9
|
103.7
|
1.0
|
|
Reference:
R.X.Zhou,
M.K.Higgins.
Scavenger Receptor CD163 Multimerises to Allow Uptake of Diverse Ligands To Be Published.
Page generated: Fri Aug 8 06:44:05 2025
|