Iron in PDB 1a4f: Bar-Headed Goose Hemoglobin (Oxy Form)
Protein crystallography data
The structure of Bar-Headed Goose Hemoglobin (Oxy Form), PDB code: 1a4f
was solved by
J.Zhang,
X.Gu,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
10.00 /
2.00
|
Space group
|
P 42 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
81.590,
81.590,
107.280,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
n/a /
n/a
|
Iron Binding Sites:
The binding sites of Iron atom in the Bar-Headed Goose Hemoglobin (Oxy Form)
(pdb code 1a4f). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
Bar-Headed Goose Hemoglobin (Oxy Form), PDB code: 1a4f:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 1a4f
Go back to
Iron Binding Sites List in 1a4f
Iron binding site 1 out
of 2 in the Bar-Headed Goose Hemoglobin (Oxy Form)
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Bar-Headed Goose Hemoglobin (Oxy Form) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe150
b:23.5
occ:1.00
|
FE
|
A:HEM150
|
0.0
|
23.5
|
1.0
|
O1
|
A:OXY151
|
1.8
|
18.1
|
1.0
|
NA
|
A:HEM150
|
2.0
|
26.1
|
1.0
|
ND
|
A:HEM150
|
2.0
|
28.5
|
1.0
|
NC
|
A:HEM150
|
2.0
|
24.4
|
1.0
|
NB
|
A:HEM150
|
2.1
|
22.8
|
1.0
|
NE2
|
A:HIS87
|
2.1
|
8.6
|
1.0
|
CD2
|
A:HIS87
|
2.9
|
20.8
|
1.0
|
O2
|
A:OXY151
|
3.0
|
43.8
|
1.0
|
C1A
|
A:HEM150
|
3.0
|
29.1
|
1.0
|
C4D
|
A:HEM150
|
3.0
|
25.0
|
1.0
|
C4A
|
A:HEM150
|
3.0
|
34.9
|
1.0
|
C1B
|
A:HEM150
|
3.1
|
22.6
|
1.0
|
C4C
|
A:HEM150
|
3.1
|
17.2
|
1.0
|
C4B
|
A:HEM150
|
3.1
|
19.6
|
1.0
|
C1C
|
A:HEM150
|
3.1
|
16.8
|
1.0
|
C1D
|
A:HEM150
|
3.1
|
24.9
|
1.0
|
CE1
|
A:HIS87
|
3.3
|
17.6
|
1.0
|
CHA
|
A:HEM150
|
3.3
|
26.4
|
1.0
|
CHC
|
A:HEM150
|
3.5
|
22.1
|
1.0
|
CHB
|
A:HEM150
|
3.5
|
27.6
|
1.0
|
CHD
|
A:HEM150
|
3.5
|
27.2
|
1.0
|
CG
|
A:HIS87
|
4.2
|
15.5
|
1.0
|
C2A
|
A:HEM150
|
4.2
|
27.6
|
1.0
|
C3A
|
A:HEM150
|
4.2
|
22.4
|
1.0
|
C3D
|
A:HEM150
|
4.3
|
27.1
|
1.0
|
C2B
|
A:HEM150
|
4.3
|
24.2
|
1.0
|
C3B
|
A:HEM150
|
4.3
|
19.8
|
1.0
|
ND1
|
A:HIS87
|
4.3
|
21.2
|
1.0
|
C3C
|
A:HEM150
|
4.3
|
19.2
|
1.0
|
C2C
|
A:HEM150
|
4.3
|
17.1
|
1.0
|
C2D
|
A:HEM150
|
4.3
|
23.3
|
1.0
|
NE2
|
A:HIS58
|
4.5
|
21.7
|
1.0
|
CE1
|
A:HIS58
|
4.8
|
26.5
|
1.0
|
|
Iron binding site 2 out
of 2 in 1a4f
Go back to
Iron Binding Sites List in 1a4f
Iron binding site 2 out
of 2 in the Bar-Headed Goose Hemoglobin (Oxy Form)
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Bar-Headed Goose Hemoglobin (Oxy Form) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe150
b:19.8
occ:1.00
|
FE
|
B:HEM150
|
0.0
|
19.8
|
1.0
|
O1
|
B:OXY151
|
1.8
|
18.8
|
1.0
|
ND
|
B:HEM150
|
2.0
|
16.7
|
1.0
|
NC
|
B:HEM150
|
2.0
|
19.2
|
1.0
|
NA
|
B:HEM150
|
2.0
|
18.7
|
1.0
|
NB
|
B:HEM150
|
2.0
|
19.2
|
1.0
|
NE2
|
B:HIS92
|
2.1
|
13.1
|
1.0
|
C4D
|
B:HEM150
|
3.0
|
17.8
|
1.0
|
O2
|
B:OXY151
|
3.0
|
28.5
|
1.0
|
C4C
|
B:HEM150
|
3.0
|
11.2
|
1.0
|
C1A
|
B:HEM150
|
3.0
|
17.6
|
1.0
|
C1B
|
B:HEM150
|
3.0
|
18.9
|
1.0
|
C4B
|
B:HEM150
|
3.1
|
16.9
|
1.0
|
CE1
|
B:HIS92
|
3.1
|
18.0
|
1.0
|
C1C
|
B:HEM150
|
3.1
|
15.2
|
1.0
|
C1D
|
B:HEM150
|
3.1
|
14.3
|
1.0
|
C4A
|
B:HEM150
|
3.1
|
16.2
|
1.0
|
CD2
|
B:HIS92
|
3.1
|
11.7
|
1.0
|
CHA
|
B:HEM150
|
3.3
|
16.5
|
1.0
|
CHC
|
B:HEM150
|
3.4
|
17.2
|
1.0
|
CHD
|
B:HEM150
|
3.4
|
18.4
|
1.0
|
CHB
|
B:HEM150
|
3.5
|
16.4
|
1.0
|
ND1
|
B:HIS92
|
4.2
|
16.9
|
1.0
|
CG
|
B:HIS92
|
4.2
|
17.6
|
1.0
|
C3C
|
B:HEM150
|
4.2
|
9.8
|
1.0
|
C3D
|
B:HEM150
|
4.2
|
16.6
|
1.0
|
C2A
|
B:HEM150
|
4.2
|
14.7
|
1.0
|
C2C
|
B:HEM150
|
4.3
|
7.4
|
1.0
|
C2B
|
B:HEM150
|
4.3
|
12.5
|
1.0
|
C2D
|
B:HEM150
|
4.3
|
13.4
|
1.0
|
C3A
|
B:HEM150
|
4.3
|
17.7
|
1.0
|
C3B
|
B:HEM150
|
4.3
|
17.1
|
1.0
|
NE2
|
B:HIS63
|
4.5
|
12.9
|
1.0
|
CG2
|
B:VAL67
|
4.9
|
18.8
|
1.0
|
CE1
|
B:HIS63
|
5.0
|
15.2
|
1.0
|
|
Reference:
J.Zhang,
Z.Hua,
J.R.Tame,
G.Lu,
R.Zhang,
X.Gu.
The Crystal Structure of A High Oxygen Affinity Species of Haemoglobin (Bar-Headed Goose Haemoglobin in the Oxy Form). J.Mol.Biol. V. 255 484 1996.
ISSN: ISSN 0022-2836
PubMed: 8568892
DOI: 10.1006/JMBI.1996.0040
Page generated: Sat Aug 3 01:59:12 2024
|