Iron in PDB 1ye1: T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAY35A Oxy (2MM Ihp, 20% Peg) (1 Test Set)
Protein crystallography data
The structure of T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAY35A Oxy (2MM Ihp, 20% Peg) (1 Test Set), PDB code: 1ye1
was solved by
J.S.Kavanaugh,
P.H.Rogers,
A.Arnone,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
10.00 /
4.50
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
96.400,
98.900,
66.900,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
29.5 /
34.3
|
Iron Binding Sites:
The binding sites of Iron atom in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAY35A Oxy (2MM Ihp, 20% Peg) (1 Test Set)
(pdb code 1ye1). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAY35A Oxy (2MM Ihp, 20% Peg) (1 Test Set), PDB code: 1ye1:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 1ye1
Go back to
Iron Binding Sites List in 1ye1
Iron binding site 1 out
of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAY35A Oxy (2MM Ihp, 20% Peg) (1 Test Set)
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAY35A Oxy (2MM Ihp, 20% Peg) (1 Test Set) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe142
b:18.6
occ:1.00
|
FE
|
A:HEM142
|
0.0
|
18.6
|
1.0
|
NA
|
A:HEM142
|
2.0
|
12.1
|
1.0
|
NC
|
A:HEM142
|
2.0
|
15.0
|
1.0
|
ND
|
A:HEM142
|
2.0
|
14.7
|
1.0
|
NB
|
A:HEM142
|
2.1
|
10.3
|
1.0
|
NE2
|
A:HIS87
|
2.2
|
11.6
|
1.0
|
CE1
|
A:HIS87
|
3.0
|
8.3
|
1.0
|
C1A
|
A:HEM142
|
3.0
|
15.6
|
1.0
|
C4D
|
A:HEM142
|
3.1
|
16.2
|
1.0
|
C1C
|
A:HEM142
|
3.1
|
16.2
|
1.0
|
C1B
|
A:HEM142
|
3.1
|
10.5
|
1.0
|
C4A
|
A:HEM142
|
3.1
|
13.0
|
1.0
|
C4C
|
A:HEM142
|
3.1
|
16.7
|
1.0
|
C4B
|
A:HEM142
|
3.1
|
11.9
|
1.0
|
C1D
|
A:HEM142
|
3.1
|
16.3
|
1.0
|
O
|
A:HOH219
|
3.2
|
19.6
|
1.0
|
CD2
|
A:HIS87
|
3.4
|
2.0
|
1.0
|
CHA
|
A:HEM142
|
3.4
|
17.1
|
1.0
|
CHC
|
A:HEM142
|
3.5
|
15.1
|
1.0
|
CHB
|
A:HEM142
|
3.5
|
9.7
|
1.0
|
CHD
|
A:HEM142
|
3.5
|
9.2
|
1.0
|
ND1
|
A:HIS87
|
4.2
|
8.5
|
1.0
|
C2A
|
A:HEM142
|
4.2
|
14.5
|
1.0
|
C3A
|
A:HEM142
|
4.3
|
12.3
|
1.0
|
C3D
|
A:HEM142
|
4.3
|
17.3
|
1.0
|
C2C
|
A:HEM142
|
4.3
|
12.2
|
1.0
|
C2B
|
A:HEM142
|
4.3
|
11.1
|
1.0
|
C3B
|
A:HEM142
|
4.3
|
14.4
|
1.0
|
C3C
|
A:HEM142
|
4.3
|
11.2
|
1.0
|
C2D
|
A:HEM142
|
4.3
|
17.0
|
1.0
|
CG
|
A:HIS87
|
4.4
|
13.3
|
1.0
|
NE2
|
A:HIS58
|
4.6
|
11.7
|
1.0
|
CD1
|
A:LEU91
|
4.6
|
13.8
|
1.0
|
CE1
|
A:HIS58
|
4.8
|
18.7
|
1.0
|
|
Iron binding site 2 out
of 4 in 1ye1
Go back to
Iron Binding Sites List in 1ye1
Iron binding site 2 out
of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAY35A Oxy (2MM Ihp, 20% Peg) (1 Test Set)
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAY35A Oxy (2MM Ihp, 20% Peg) (1 Test Set) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe147
b:12.5
occ:1.00
|
FE
|
B:HEM147
|
0.0
|
12.5
|
1.0
|
ND
|
B:HEM147
|
2.0
|
4.2
|
1.0
|
NB
|
B:HEM147
|
2.0
|
2.0
|
1.0
|
NC
|
B:HEM147
|
2.0
|
6.3
|
1.0
|
NA
|
B:HEM147
|
2.0
|
8.3
|
1.0
|
NE2
|
B:HIS92
|
2.2
|
15.8
|
1.0
|
C4B
|
B:HEM147
|
3.0
|
3.7
|
1.0
|
CE1
|
B:HIS92
|
3.0
|
7.3
|
1.0
|
C1D
|
B:HEM147
|
3.0
|
8.4
|
1.0
|
C4C
|
B:HEM147
|
3.0
|
4.7
|
1.0
|
C1A
|
B:HEM147
|
3.1
|
7.1
|
1.0
|
C4D
|
B:HEM147
|
3.1
|
7.5
|
1.0
|
C1C
|
B:HEM147
|
3.1
|
2.1
|
1.0
|
C4A
|
B:HEM147
|
3.1
|
4.2
|
1.0
|
C1B
|
B:HEM147
|
3.1
|
4.5
|
1.0
|
CD2
|
B:HIS92
|
3.3
|
15.0
|
1.0
|
CHD
|
B:HEM147
|
3.4
|
5.9
|
1.0
|
CHC
|
B:HEM147
|
3.4
|
6.5
|
1.0
|
CHB
|
B:HEM147
|
3.5
|
6.6
|
1.0
|
CHA
|
B:HEM147
|
3.5
|
10.4
|
1.0
|
ND1
|
B:HIS92
|
4.2
|
9.7
|
1.0
|
C3B
|
B:HEM147
|
4.2
|
2.0
|
1.0
|
C2B
|
B:HEM147
|
4.3
|
2.0
|
1.0
|
C3D
|
B:HEM147
|
4.3
|
4.2
|
1.0
|
C2D
|
B:HEM147
|
4.3
|
6.1
|
1.0
|
C3C
|
B:HEM147
|
4.3
|
9.2
|
1.0
|
C2A
|
B:HEM147
|
4.3
|
8.1
|
1.0
|
C2C
|
B:HEM147
|
4.3
|
8.4
|
1.0
|
C3A
|
B:HEM147
|
4.3
|
11.5
|
1.0
|
CG
|
B:HIS92
|
4.4
|
9.8
|
1.0
|
NE2
|
B:HIS63
|
4.5
|
18.5
|
1.0
|
CG2
|
B:VAL67
|
4.6
|
2.0
|
1.0
|
CD1
|
B:LEU96
|
4.9
|
5.8
|
1.0
|
|
Iron binding site 3 out
of 4 in 1ye1
Go back to
Iron Binding Sites List in 1ye1
Iron binding site 3 out
of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAY35A Oxy (2MM Ihp, 20% Peg) (1 Test Set)
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAY35A Oxy (2MM Ihp, 20% Peg) (1 Test Set) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe142
b:16.2
occ:1.00
|
FE
|
C:HEM142
|
0.0
|
16.2
|
1.0
|
ND
|
C:HEM142
|
2.0
|
5.7
|
1.0
|
NC
|
C:HEM142
|
2.0
|
8.3
|
1.0
|
NA
|
C:HEM142
|
2.0
|
10.0
|
1.0
|
NB
|
C:HEM142
|
2.1
|
14.1
|
1.0
|
NE2
|
C:HIS87
|
2.2
|
9.2
|
1.0
|
CE1
|
C:HIS87
|
2.9
|
14.1
|
1.0
|
C1D
|
C:HEM142
|
3.0
|
5.8
|
1.0
|
C4C
|
C:HEM142
|
3.0
|
6.2
|
1.0
|
C4D
|
C:HEM142
|
3.0
|
11.1
|
1.0
|
C1A
|
C:HEM142
|
3.0
|
15.1
|
1.0
|
C1C
|
C:HEM142
|
3.1
|
10.3
|
1.0
|
C4A
|
C:HEM142
|
3.1
|
15.0
|
1.0
|
C1B
|
C:HEM142
|
3.1
|
8.9
|
1.0
|
C4B
|
C:HEM142
|
3.1
|
11.8
|
1.0
|
CHD
|
C:HEM142
|
3.4
|
6.5
|
1.0
|
CD2
|
C:HIS87
|
3.4
|
10.7
|
1.0
|
CHA
|
C:HEM142
|
3.4
|
11.6
|
1.0
|
O
|
C:HOH256
|
3.5
|
18.5
|
1.0
|
CHC
|
C:HEM142
|
3.5
|
12.2
|
1.0
|
CHB
|
C:HEM142
|
3.5
|
10.8
|
1.0
|
ND1
|
C:HIS87
|
4.2
|
11.4
|
1.0
|
C3D
|
C:HEM142
|
4.3
|
10.4
|
1.0
|
C2D
|
C:HEM142
|
4.3
|
9.0
|
1.0
|
C3C
|
C:HEM142
|
4.3
|
6.2
|
1.0
|
C2A
|
C:HEM142
|
4.3
|
16.3
|
1.0
|
C2C
|
C:HEM142
|
4.3
|
8.6
|
1.0
|
C3B
|
C:HEM142
|
4.3
|
13.2
|
1.0
|
C3A
|
C:HEM142
|
4.3
|
19.1
|
1.0
|
C2B
|
C:HEM142
|
4.3
|
12.9
|
1.0
|
CG
|
C:HIS87
|
4.4
|
10.5
|
1.0
|
CD1
|
C:LEU91
|
4.4
|
16.5
|
1.0
|
CE1
|
C:HIS58
|
4.7
|
11.2
|
1.0
|
NE2
|
C:HIS58
|
4.7
|
12.7
|
1.0
|
|
Iron binding site 4 out
of 4 in 1ye1
Go back to
Iron Binding Sites List in 1ye1
Iron binding site 4 out
of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAY35A Oxy (2MM Ihp, 20% Peg) (1 Test Set)
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAY35A Oxy (2MM Ihp, 20% Peg) (1 Test Set) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe147
b:19.4
occ:1.00
|
FE
|
D:HEM147
|
0.0
|
19.4
|
1.0
|
ND
|
D:HEM147
|
2.0
|
13.5
|
1.0
|
NB
|
D:HEM147
|
2.0
|
13.3
|
1.0
|
NA
|
D:HEM147
|
2.0
|
21.0
|
1.0
|
NC
|
D:HEM147
|
2.0
|
12.7
|
1.0
|
NE2
|
D:HIS92
|
2.2
|
18.7
|
1.0
|
C4D
|
D:HEM147
|
3.0
|
18.5
|
1.0
|
C1D
|
D:HEM147
|
3.0
|
18.5
|
1.0
|
C1B
|
D:HEM147
|
3.1
|
15.0
|
1.0
|
C4B
|
D:HEM147
|
3.1
|
15.6
|
1.0
|
CE1
|
D:HIS92
|
3.1
|
25.3
|
1.0
|
C4A
|
D:HEM147
|
3.1
|
19.0
|
1.0
|
C1A
|
D:HEM147
|
3.1
|
15.9
|
1.0
|
C1C
|
D:HEM147
|
3.1
|
12.2
|
1.0
|
C4C
|
D:HEM147
|
3.1
|
11.4
|
1.0
|
CD2
|
D:HIS92
|
3.4
|
18.6
|
1.0
|
CHA
|
D:HEM147
|
3.4
|
15.6
|
1.0
|
CHC
|
D:HEM147
|
3.4
|
15.6
|
1.0
|
CHB
|
D:HEM147
|
3.4
|
16.1
|
1.0
|
CHD
|
D:HEM147
|
3.5
|
13.3
|
1.0
|
CG2
|
D:VAL67
|
4.1
|
18.1
|
1.0
|
C3D
|
D:HEM147
|
4.2
|
18.5
|
1.0
|
C2D
|
D:HEM147
|
4.3
|
16.2
|
1.0
|
ND1
|
D:HIS92
|
4.3
|
15.6
|
1.0
|
C2B
|
D:HEM147
|
4.3
|
16.3
|
1.0
|
C3B
|
D:HEM147
|
4.3
|
14.6
|
1.0
|
C3A
|
D:HEM147
|
4.3
|
19.9
|
1.0
|
C2A
|
D:HEM147
|
4.3
|
20.1
|
1.0
|
C3C
|
D:HEM147
|
4.3
|
10.3
|
1.0
|
C2C
|
D:HEM147
|
4.3
|
10.3
|
1.0
|
NE2
|
D:HIS63
|
4.3
|
27.7
|
1.0
|
CG
|
D:HIS92
|
4.4
|
15.4
|
1.0
|
CE1
|
D:HIS63
|
4.5
|
31.2
|
1.0
|
CD1
|
D:LEU96
|
4.9
|
16.1
|
1.0
|
|
Reference:
J.S.Kavanaugh,
P.H.Rogers,
A.Arnone.
Crystallographic Evidence For A New Ensemble of Ligand-Induced Allosteric Transitions in Hemoglobin: the T-to-T(High) Quaternary Transitions. Biochemistry V. 44 6101 2005.
ISSN: ISSN 0006-2960
PubMed: 15835899
DOI: 10.1021/BI047813A
Page generated: Sat Aug 3 17:32:54 2024
|