Iron in PDB 2y4f: X-Ray Crystallographic Structure of E. Coli Heme-Efeb
Protein crystallography data
The structure of X-Ray Crystallographic Structure of E. Coli Heme-Efeb, PDB code: 2y4f
was solved by
V.A.Bamford,
S.C.Andrews,
K.A.Watson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
60.00 /
2.70
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
83.330,
85.930,
120.000,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.3 /
28.4
|
Iron Binding Sites:
The binding sites of Iron atom in the X-Ray Crystallographic Structure of E. Coli Heme-Efeb
(pdb code 2y4f). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
X-Ray Crystallographic Structure of E. Coli Heme-Efeb, PDB code: 2y4f:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 2y4f
Go back to
Iron Binding Sites List in 2y4f
Iron binding site 1 out
of 2 in the X-Ray Crystallographic Structure of E. Coli Heme-Efeb
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of X-Ray Crystallographic Structure of E. Coli Heme-Efeb within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe389
b:21.3
occ:1.00
|
FE
|
A:HEM389
|
0.0
|
21.3
|
1.0
|
NA
|
A:HEM389
|
2.0
|
18.9
|
1.0
|
NC
|
A:HEM389
|
2.0
|
18.9
|
1.0
|
NB
|
A:HEM389
|
2.0
|
19.8
|
1.0
|
ND
|
A:HEM389
|
2.0
|
19.4
|
1.0
|
NE2
|
A:HIS294
|
2.2
|
34.6
|
1.0
|
C1A
|
A:HEM389
|
3.0
|
19.4
|
1.0
|
C4D
|
A:HEM389
|
3.0
|
20.3
|
1.0
|
C4B
|
A:HEM389
|
3.0
|
19.1
|
1.0
|
C1C
|
A:HEM389
|
3.0
|
17.2
|
1.0
|
C4A
|
A:HEM389
|
3.1
|
18.4
|
1.0
|
C4C
|
A:HEM389
|
3.1
|
18.5
|
1.0
|
O
|
A:HOH2104
|
3.1
|
5.2
|
1.0
|
C1B
|
A:HEM389
|
3.1
|
20.1
|
1.0
|
C1D
|
A:HEM389
|
3.1
|
18.9
|
1.0
|
CE1
|
A:HIS294
|
3.2
|
34.4
|
1.0
|
CD2
|
A:HIS294
|
3.2
|
34.4
|
1.0
|
CHA
|
A:HEM389
|
3.3
|
20.2
|
1.0
|
CHC
|
A:HEM389
|
3.4
|
17.0
|
1.0
|
CHD
|
A:HEM389
|
3.5
|
18.4
|
1.0
|
CHB
|
A:HEM389
|
3.5
|
19.2
|
1.0
|
NH1
|
A:ARG312
|
4.0
|
15.4
|
1.0
|
C2A
|
A:HEM389
|
4.2
|
17.5
|
1.0
|
C3B
|
A:HEM389
|
4.2
|
20.8
|
1.0
|
C3A
|
A:HEM389
|
4.2
|
17.7
|
1.0
|
C2C
|
A:HEM389
|
4.3
|
16.7
|
1.0
|
C3D
|
A:HEM389
|
4.3
|
21.0
|
1.0
|
C2B
|
A:HEM389
|
4.3
|
19.8
|
1.0
|
C3C
|
A:HEM389
|
4.3
|
17.7
|
1.0
|
ND1
|
A:HIS294
|
4.3
|
32.3
|
1.0
|
C2D
|
A:HEM389
|
4.3
|
19.4
|
1.0
|
CG
|
A:HIS294
|
4.3
|
32.7
|
1.0
|
CD
|
A:ARG312
|
4.6
|
15.7
|
1.0
|
CZ
|
A:ARG312
|
4.7
|
16.5
|
1.0
|
NE
|
A:ARG312
|
5.0
|
15.3
|
1.0
|
CE2
|
A:PHE333
|
5.0
|
11.2
|
1.0
|
|
Iron binding site 2 out
of 2 in 2y4f
Go back to
Iron Binding Sites List in 2y4f
Iron binding site 2 out
of 2 in the X-Ray Crystallographic Structure of E. Coli Heme-Efeb
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of X-Ray Crystallographic Structure of E. Coli Heme-Efeb within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe389
b:26.3
occ:1.00
|
FE
|
B:HEM389
|
0.0
|
26.3
|
1.0
|
NA
|
B:HEM389
|
2.0
|
25.9
|
1.0
|
NB
|
B:HEM389
|
2.0
|
24.8
|
1.0
|
NE2
|
B:HIS294
|
2.1
|
28.4
|
1.0
|
NC
|
B:HEM389
|
2.1
|
27.0
|
1.0
|
ND
|
B:HEM389
|
2.1
|
26.3
|
1.0
|
O
|
B:HOH2090
|
2.7
|
23.1
|
1.0
|
C4A
|
B:HEM389
|
3.0
|
25.5
|
1.0
|
C1A
|
B:HEM389
|
3.0
|
26.0
|
1.0
|
C4B
|
B:HEM389
|
3.0
|
24.6
|
1.0
|
CE1
|
B:HIS294
|
3.0
|
28.8
|
1.0
|
C1B
|
B:HEM389
|
3.0
|
23.7
|
1.0
|
CD2
|
B:HIS294
|
3.0
|
28.6
|
1.0
|
C1C
|
B:HEM389
|
3.1
|
26.0
|
1.0
|
C4C
|
B:HEM389
|
3.1
|
26.5
|
1.0
|
C4D
|
B:HEM389
|
3.1
|
27.0
|
1.0
|
C1D
|
B:HEM389
|
3.1
|
26.1
|
1.0
|
CHB
|
B:HEM389
|
3.4
|
24.1
|
1.0
|
CHA
|
B:HEM389
|
3.4
|
26.2
|
1.0
|
CHC
|
B:HEM389
|
3.4
|
24.8
|
1.0
|
CHD
|
B:HEM389
|
3.5
|
26.7
|
1.0
|
ND1
|
B:HIS294
|
4.1
|
29.4
|
1.0
|
NH1
|
B:ARG312
|
4.2
|
24.8
|
1.0
|
CG
|
B:HIS294
|
4.2
|
29.5
|
1.0
|
C3A
|
B:HEM389
|
4.2
|
25.6
|
1.0
|
C2A
|
B:HEM389
|
4.2
|
25.7
|
1.0
|
C3B
|
B:HEM389
|
4.2
|
23.3
|
1.0
|
C2B
|
B:HEM389
|
4.2
|
23.1
|
1.0
|
C2C
|
B:HEM389
|
4.3
|
25.8
|
1.0
|
C3C
|
B:HEM389
|
4.3
|
25.9
|
1.0
|
C2D
|
B:HEM389
|
4.4
|
25.5
|
1.0
|
C3D
|
B:HEM389
|
4.4
|
26.1
|
1.0
|
CD
|
B:ARG312
|
4.8
|
23.4
|
1.0
|
CE2
|
B:PHE333
|
5.0
|
19.7
|
1.0
|
|
Reference:
V.A.Bamford,
S.C.Andrews,
K.A.Watson.
Efeb, the Peroxidase Component of the Efeuob Bacterial Fe(II) Transport System, Also Shows Novel Removal of Iron From Heme To Be Published.
Page generated: Sun Aug 4 05:05:25 2024
|