Iron in PDB 8wiy: Cryo-Em Structure of Alligator Haemoglobin in Oxy Form
Iron Binding Sites:
The binding sites of Iron atom in the Cryo-Em Structure of Alligator Haemoglobin in Oxy Form
(pdb code 8wiy). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
Cryo-Em Structure of Alligator Haemoglobin in Oxy Form, PDB code: 8wiy:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 8wiy
Go back to
Iron Binding Sites List in 8wiy
Iron binding site 1 out
of 2 in the Cryo-Em Structure of Alligator Haemoglobin in Oxy Form
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Cryo-Em Structure of Alligator Haemoglobin in Oxy Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe201
b:21.8
occ:1.00
|
FE
|
A:HEM201
|
0.0
|
21.8
|
1.0
|
ND
|
A:HEM201
|
2.0
|
27.5
|
1.0
|
NA
|
A:HEM201
|
2.0
|
21.2
|
1.0
|
O2
|
A:OXY202
|
2.0
|
44.1
|
1.0
|
NC
|
A:HEM201
|
2.0
|
22.4
|
1.0
|
NB
|
A:HEM201
|
2.1
|
22.1
|
1.0
|
NE2
|
A:HIS87
|
2.2
|
29.5
|
1.0
|
C1D
|
A:HEM201
|
3.0
|
23.8
|
1.0
|
C4D
|
A:HEM201
|
3.0
|
28.0
|
1.0
|
C1A
|
A:HEM201
|
3.0
|
22.5
|
1.0
|
C4B
|
A:HEM201
|
3.0
|
26.3
|
1.0
|
O1
|
A:OXY202
|
3.0
|
64.8
|
1.0
|
C4A
|
A:HEM201
|
3.0
|
21.3
|
1.0
|
C1C
|
A:HEM201
|
3.0
|
28.4
|
1.0
|
C4C
|
A:HEM201
|
3.0
|
24.0
|
1.0
|
C1B
|
A:HEM201
|
3.1
|
20.4
|
1.0
|
CE1
|
A:HIS87
|
3.1
|
31.3
|
1.0
|
CD2
|
A:HIS87
|
3.2
|
28.9
|
1.0
|
CHA
|
A:HEM201
|
3.4
|
25.6
|
1.0
|
CHD
|
A:HEM201
|
3.4
|
21.4
|
1.0
|
CHC
|
A:HEM201
|
3.4
|
24.1
|
1.0
|
CHB
|
A:HEM201
|
3.5
|
19.8
|
1.0
|
C2A
|
A:HEM201
|
4.2
|
24.3
|
1.0
|
C3A
|
A:HEM201
|
4.2
|
23.5
|
1.0
|
C2D
|
A:HEM201
|
4.2
|
29.3
|
1.0
|
C3D
|
A:HEM201
|
4.2
|
30.8
|
1.0
|
C2C
|
A:HEM201
|
4.3
|
26.8
|
1.0
|
ND1
|
A:HIS87
|
4.3
|
31.3
|
1.0
|
C3C
|
A:HEM201
|
4.3
|
25.1
|
1.0
|
C2B
|
A:HEM201
|
4.3
|
23.4
|
1.0
|
C3B
|
A:HEM201
|
4.3
|
25.8
|
1.0
|
NE2
|
A:HIS58
|
4.3
|
33.6
|
1.0
|
CG
|
A:HIS87
|
4.3
|
34.5
|
1.0
|
CE1
|
A:HIS58
|
4.5
|
35.3
|
1.0
|
CG2
|
A:VAL62
|
4.9
|
21.9
|
1.0
|
|
Iron binding site 2 out
of 2 in 8wiy
Go back to
Iron Binding Sites List in 8wiy
Iron binding site 2 out
of 2 in the Cryo-Em Structure of Alligator Haemoglobin in Oxy Form
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Cryo-Em Structure of Alligator Haemoglobin in Oxy Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe201
b:22.9
occ:1.00
|
FE
|
B:HEM201
|
0.0
|
22.9
|
1.0
|
ND
|
B:HEM201
|
2.0
|
28.2
|
1.0
|
NA
|
B:HEM201
|
2.0
|
20.8
|
1.0
|
O1
|
B:OXY202
|
2.0
|
55.3
|
1.0
|
NC
|
B:HEM201
|
2.0
|
23.7
|
1.0
|
NB
|
B:HEM201
|
2.1
|
24.0
|
1.0
|
NE2
|
B:HIS92
|
2.2
|
28.6
|
1.0
|
C4D
|
B:HEM201
|
3.0
|
28.3
|
1.0
|
C1A
|
B:HEM201
|
3.0
|
24.7
|
1.0
|
C1D
|
B:HEM201
|
3.0
|
23.9
|
1.0
|
O2
|
B:OXY202
|
3.0
|
64.4
|
1.0
|
C4A
|
B:HEM201
|
3.0
|
23.2
|
1.0
|
C4B
|
B:HEM201
|
3.0
|
28.7
|
1.0
|
C4C
|
B:HEM201
|
3.1
|
27.9
|
1.0
|
C1B
|
B:HEM201
|
3.1
|
22.2
|
1.0
|
C1C
|
B:HEM201
|
3.1
|
29.9
|
1.0
|
CE1
|
B:HIS92
|
3.2
|
30.3
|
1.0
|
CD2
|
B:HIS92
|
3.2
|
29.4
|
1.0
|
CHC
|
B:HEM201
|
3.4
|
30.9
|
1.0
|
CHA
|
B:HEM201
|
3.4
|
28.5
|
1.0
|
CHD
|
B:HEM201
|
3.5
|
23.7
|
1.0
|
CHB
|
B:HEM201
|
3.5
|
21.1
|
1.0
|
C2A
|
B:HEM201
|
4.2
|
28.6
|
1.0
|
C2D
|
B:HEM201
|
4.2
|
31.2
|
1.0
|
C3D
|
B:HEM201
|
4.2
|
32.3
|
1.0
|
C3A
|
B:HEM201
|
4.2
|
26.2
|
1.0
|
C2B
|
B:HEM201
|
4.3
|
29.7
|
1.0
|
C3C
|
B:HEM201
|
4.3
|
31.9
|
1.0
|
C2C
|
B:HEM201
|
4.3
|
32.6
|
1.0
|
C3B
|
B:HEM201
|
4.3
|
30.7
|
1.0
|
ND1
|
B:HIS92
|
4.3
|
30.2
|
1.0
|
CG
|
B:HIS92
|
4.4
|
32.8
|
1.0
|
NE2
|
B:HIS63
|
4.6
|
26.6
|
1.0
|
CG2
|
B:VAL67
|
4.7
|
27.3
|
1.0
|
|
Reference:
K.Takahashi,
Y.Lee,
A.Fago,
N.M.Bautista,
J.F.Storz,
A.Kawamoto,
G.Kurisu,
T.Nishizawa,
J.R.H.Tame.
The Unique Allosteric Property of Crocodilian Haemoglobin Elucidated By Cryo-Em. Nat Commun V. 15 6505 2024.
ISSN: ESSN 2041-1723
PubMed: 39090102
DOI: 10.1038/S41467-024-49947-X
Page generated: Sat Sep 28 21:51:57 2024
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