Iron in PDB 6kaq: Carbonmonoxy Human Hemoglobin C in the R Quaternary Structure at 140 K: Dark
Protein crystallography data
The structure of Carbonmonoxy Human Hemoglobin C in the R Quaternary Structure at 140 K: Dark, PDB code: 6kaq
was solved by
N.Shibayama,
S.Y.Park,
M.Ohki,
A.Sato-Tomita,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
19.21 /
1.50
|
Space group
|
P 41 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
53.583,
53.583,
192.812,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.2 /
22
|
Iron Binding Sites:
The binding sites of Iron atom in the Carbonmonoxy Human Hemoglobin C in the R Quaternary Structure at 140 K: Dark
(pdb code 6kaq). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
Carbonmonoxy Human Hemoglobin C in the R Quaternary Structure at 140 K: Dark, PDB code: 6kaq:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 6kaq
Go back to
Iron Binding Sites List in 6kaq
Iron binding site 1 out
of 2 in the Carbonmonoxy Human Hemoglobin C in the R Quaternary Structure at 140 K: Dark
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Carbonmonoxy Human Hemoglobin C in the R Quaternary Structure at 140 K: Dark within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe201
b:15.9
occ:1.00
|
FE
|
A:HEM201
|
0.0
|
15.9
|
1.0
|
C
|
A:CMO202
|
1.7
|
15.3
|
1.0
|
NA
|
A:HEM201
|
2.0
|
15.2
|
1.0
|
NE2
|
A:HIS87
|
2.0
|
15.4
|
1.0
|
NB
|
A:HEM201
|
2.0
|
12.6
|
1.0
|
NC
|
A:HEM201
|
2.1
|
14.7
|
1.0
|
ND
|
A:HEM201
|
2.1
|
16.7
|
1.0
|
O
|
A:CMO202
|
2.9
|
17.6
|
1.0
|
CE1
|
A:HIS87
|
3.0
|
17.7
|
1.0
|
C1A
|
A:HEM201
|
3.0
|
16.2
|
1.0
|
C4A
|
A:HEM201
|
3.1
|
15.6
|
1.0
|
C1B
|
A:HEM201
|
3.1
|
15.1
|
1.0
|
C4D
|
A:HEM201
|
3.1
|
17.2
|
1.0
|
C4B
|
A:HEM201
|
3.1
|
13.1
|
1.0
|
C1C
|
A:HEM201
|
3.1
|
15.9
|
1.0
|
CD2
|
A:HIS87
|
3.1
|
17.0
|
1.0
|
C4C
|
A:HEM201
|
3.1
|
13.5
|
1.0
|
C1D
|
A:HEM201
|
3.1
|
17.3
|
1.0
|
CHA
|
A:HEM201
|
3.4
|
18.7
|
1.0
|
CHB
|
A:HEM201
|
3.5
|
16.0
|
1.0
|
CHC
|
A:HEM201
|
3.5
|
15.6
|
1.0
|
CHD
|
A:HEM201
|
3.5
|
17.7
|
1.0
|
ND1
|
A:HIS87
|
4.1
|
16.9
|
1.0
|
CG
|
A:HIS87
|
4.2
|
16.3
|
1.0
|
C2A
|
A:HEM201
|
4.3
|
18.9
|
1.0
|
C3A
|
A:HEM201
|
4.3
|
17.1
|
1.0
|
C3C
|
A:HEM201
|
4.3
|
15.2
|
1.0
|
C2B
|
A:HEM201
|
4.3
|
15.6
|
1.0
|
C2C
|
A:HEM201
|
4.3
|
13.6
|
1.0
|
C2D
|
A:HEM201
|
4.3
|
19.6
|
1.0
|
C3B
|
A:HEM201
|
4.3
|
14.3
|
1.0
|
C3D
|
A:HEM201
|
4.3
|
17.2
|
1.0
|
NE2
|
A:HIS58
|
4.4
|
22.3
|
1.0
|
|
Iron binding site 2 out
of 2 in 6kaq
Go back to
Iron Binding Sites List in 6kaq
Iron binding site 2 out
of 2 in the Carbonmonoxy Human Hemoglobin C in the R Quaternary Structure at 140 K: Dark
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Carbonmonoxy Human Hemoglobin C in the R Quaternary Structure at 140 K: Dark within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe201
b:21.0
occ:1.00
|
FE
|
B:HEM201
|
0.0
|
21.0
|
1.0
|
C
|
B:CMO202
|
1.7
|
20.0
|
1.0
|
NE2
|
B:HIS92
|
2.0
|
22.1
|
1.0
|
NC
|
B:HEM201
|
2.0
|
19.2
|
1.0
|
NA
|
B:HEM201
|
2.1
|
19.8
|
1.0
|
NB
|
B:HEM201
|
2.1
|
18.7
|
1.0
|
ND
|
B:HEM201
|
2.1
|
23.3
|
1.0
|
O
|
B:CMO202
|
2.9
|
26.4
|
1.0
|
CE1
|
B:HIS92
|
3.0
|
24.4
|
1.0
|
C1C
|
B:HEM201
|
3.1
|
19.8
|
1.0
|
C4A
|
B:HEM201
|
3.1
|
20.3
|
1.0
|
C4C
|
B:HEM201
|
3.1
|
22.0
|
1.0
|
CD2
|
B:HIS92
|
3.1
|
22.8
|
1.0
|
C1A
|
B:HEM201
|
3.1
|
21.3
|
1.0
|
C4B
|
B:HEM201
|
3.1
|
20.8
|
1.0
|
C4D
|
B:HEM201
|
3.1
|
21.5
|
1.0
|
C1B
|
B:HEM201
|
3.1
|
20.1
|
1.0
|
C1D
|
B:HEM201
|
3.1
|
24.7
|
1.0
|
CHC
|
B:HEM201
|
3.5
|
20.5
|
1.0
|
CHA
|
B:HEM201
|
3.5
|
23.6
|
1.0
|
CHB
|
B:HEM201
|
3.5
|
22.3
|
1.0
|
CHD
|
B:HEM201
|
3.5
|
24.7
|
1.0
|
ND1
|
B:HIS92
|
4.1
|
23.3
|
1.0
|
CG
|
B:HIS92
|
4.2
|
20.1
|
1.0
|
C2C
|
B:HEM201
|
4.2
|
21.4
|
1.0
|
C3A
|
B:HEM201
|
4.3
|
21.9
|
1.0
|
C3C
|
B:HEM201
|
4.3
|
20.5
|
1.0
|
C2A
|
B:HEM201
|
4.3
|
26.4
|
1.0
|
C3B
|
B:HEM201
|
4.3
|
19.8
|
1.0
|
C3D
|
B:HEM201
|
4.3
|
22.0
|
1.0
|
C2B
|
B:HEM201
|
4.3
|
21.6
|
1.0
|
C2D
|
B:HEM201
|
4.3
|
22.6
|
1.0
|
NE2
|
B:HIS63
|
4.5
|
46.5
|
1.0
|
CG2
|
B:VAL67
|
4.7
|
51.3
|
1.0
|
|
Reference:
N.Shibayama,
A.Sato-Tomita,
M.Ohki,
K.Ichiyanagi,
S.Y.Park.
Direct Observation of Ligand Migration Within Human Hemoglobin at Work Proc.Natl.Acad.Sci.Usa 2020.
ISSN: ESSN 1091-6490
Page generated: Sun Dec 13 16:36:38 2020
|