Iron in PDB 4y8w: Crystal Structure of Human Cytochrome P450 21A2 Progesterone Complex
Protein crystallography data
The structure of Crystal Structure of Human Cytochrome P450 21A2 Progesterone Complex, PDB code: 4y8w
was solved by
P.S.Pallan,
L.Lei,
M.Egli,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
2.64
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
150.383,
86.860,
108.923,
90.00,
102.11,
90.00
|
R / Rfree (%)
|
23.1 /
28.1
|
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Human Cytochrome P450 21A2 Progesterone Complex
(pdb code 4y8w). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the
Crystal Structure of Human Cytochrome P450 21A2 Progesterone Complex, PDB code: 4y8w:
Jump to Iron binding site number:
1;
2;
3;
Iron binding site 1 out
of 3 in 4y8w
Go back to
Iron Binding Sites List in 4y8w
Iron binding site 1 out
of 3 in the Crystal Structure of Human Cytochrome P450 21A2 Progesterone Complex
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Crystal Structure of Human Cytochrome P450 21A2 Progesterone Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe603
b:25.7
occ:1.00
|
FE
|
A:HEM603
|
0.0
|
25.7
|
1.0
|
ND
|
A:HEM603
|
1.9
|
25.8
|
1.0
|
NA
|
A:HEM603
|
2.0
|
25.9
|
1.0
|
NC
|
A:HEM603
|
2.1
|
25.8
|
1.0
|
NB
|
A:HEM603
|
2.1
|
26.6
|
1.0
|
SG
|
A:CYS429
|
2.2
|
26.4
|
1.0
|
C4D
|
A:HEM603
|
2.9
|
25.4
|
1.0
|
C1D
|
A:HEM603
|
2.9
|
25.5
|
1.0
|
C1A
|
A:HEM603
|
3.0
|
25.8
|
1.0
|
C4A
|
A:HEM603
|
3.0
|
26.0
|
1.0
|
C4C
|
A:HEM603
|
3.1
|
25.8
|
1.0
|
C1B
|
A:HEM603
|
3.1
|
26.6
|
1.0
|
C4B
|
A:HEM603
|
3.1
|
26.7
|
1.0
|
C1C
|
A:HEM603
|
3.1
|
25.8
|
1.0
|
CHA
|
A:HEM603
|
3.4
|
25.6
|
1.0
|
CHD
|
A:HEM603
|
3.4
|
25.7
|
1.0
|
CB
|
A:CYS429
|
3.4
|
27.5
|
1.0
|
CHB
|
A:HEM603
|
3.5
|
26.3
|
1.0
|
CHC
|
A:HEM603
|
3.5
|
26.4
|
1.0
|
C21
|
A:STR604
|
4.0
|
31.7
|
1.0
|
CA
|
A:CYS429
|
4.1
|
27.9
|
1.0
|
C3D
|
A:HEM603
|
4.2
|
25.2
|
1.0
|
C2D
|
A:HEM603
|
4.2
|
25.4
|
1.0
|
C2A
|
A:HEM603
|
4.2
|
26.1
|
1.0
|
C3A
|
A:HEM603
|
4.2
|
25.9
|
1.0
|
C3C
|
A:HEM603
|
4.3
|
25.5
|
1.0
|
C2C
|
A:HEM603
|
4.3
|
25.5
|
1.0
|
C2B
|
A:HEM603
|
4.3
|
26.9
|
1.0
|
C3B
|
A:HEM603
|
4.4
|
26.9
|
1.0
|
O
|
A:GLY292
|
4.4
|
32.7
|
1.0
|
N
|
A:LEU430
|
4.8
|
29.1
|
1.0
|
C
|
A:CYS429
|
4.8
|
28.4
|
1.0
|
C16
|
A:STR604
|
4.8
|
31.5
|
1.0
|
N
|
A:GLY431
|
4.9
|
29.7
|
1.0
|
|
Iron binding site 2 out
of 3 in 4y8w
Go back to
Iron Binding Sites List in 4y8w
Iron binding site 2 out
of 3 in the Crystal Structure of Human Cytochrome P450 21A2 Progesterone Complex
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Crystal Structure of Human Cytochrome P450 21A2 Progesterone Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe602
b:27.3
occ:1.00
|
FE
|
B:HEM602
|
0.0
|
27.3
|
1.0
|
ND
|
B:HEM602
|
1.9
|
27.4
|
1.0
|
NA
|
B:HEM602
|
2.0
|
27.5
|
1.0
|
NC
|
B:HEM602
|
2.1
|
27.5
|
1.0
|
NB
|
B:HEM602
|
2.1
|
28.1
|
1.0
|
SG
|
B:CYS429
|
2.3
|
28.6
|
1.0
|
C4D
|
B:HEM602
|
2.9
|
27.5
|
1.0
|
C1D
|
B:HEM602
|
2.9
|
27.5
|
1.0
|
C1A
|
B:HEM602
|
3.0
|
27.4
|
1.0
|
C4C
|
B:HEM602
|
3.1
|
27.6
|
1.0
|
C4A
|
B:HEM602
|
3.1
|
27.1
|
1.0
|
C1B
|
B:HEM602
|
3.1
|
27.7
|
1.0
|
C4B
|
B:HEM602
|
3.1
|
28.3
|
1.0
|
C1C
|
B:HEM602
|
3.1
|
27.8
|
1.0
|
CHA
|
B:HEM602
|
3.4
|
27.6
|
1.0
|
CB
|
B:CYS429
|
3.4
|
29.7
|
1.0
|
CHD
|
B:HEM602
|
3.4
|
27.6
|
1.0
|
CHB
|
B:HEM602
|
3.5
|
27.2
|
1.0
|
CHC
|
B:HEM602
|
3.5
|
28.0
|
1.0
|
CA
|
B:CYS429
|
4.0
|
30.2
|
1.0
|
C21
|
B:STR603
|
4.1
|
33.8
|
1.0
|
C3D
|
B:HEM602
|
4.2
|
27.5
|
1.0
|
C2D
|
B:HEM602
|
4.2
|
27.5
|
1.0
|
C2A
|
B:HEM602
|
4.2
|
27.6
|
1.0
|
C3A
|
B:HEM602
|
4.2
|
27.2
|
1.0
|
C3C
|
B:HEM602
|
4.3
|
27.6
|
1.0
|
C2C
|
B:HEM602
|
4.3
|
27.9
|
1.0
|
C2B
|
B:HEM602
|
4.3
|
28.2
|
1.0
|
C3B
|
B:HEM602
|
4.4
|
28.4
|
1.0
|
O
|
B:GLY292
|
4.5
|
31.4
|
1.0
|
C
|
B:CYS429
|
4.8
|
30.9
|
1.0
|
CG2
|
B:THR296
|
4.9
|
35.2
|
1.0
|
C16
|
B:STR603
|
4.9
|
31.6
|
1.0
|
N
|
B:LEU430
|
4.9
|
31.6
|
1.0
|
|
Iron binding site 3 out
of 3 in 4y8w
Go back to
Iron Binding Sites List in 4y8w
Iron binding site 3 out
of 3 in the Crystal Structure of Human Cytochrome P450 21A2 Progesterone Complex
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Crystal Structure of Human Cytochrome P450 21A2 Progesterone Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe602
b:25.6
occ:1.00
|
FE
|
C:HEM602
|
0.0
|
25.6
|
1.0
|
ND
|
C:HEM602
|
1.9
|
25.8
|
1.0
|
NA
|
C:HEM602
|
2.0
|
26.0
|
1.0
|
NC
|
C:HEM602
|
2.1
|
25.9
|
1.0
|
NB
|
C:HEM602
|
2.1
|
25.9
|
1.0
|
SG
|
C:CYS429
|
2.3
|
26.6
|
1.0
|
C4D
|
C:HEM602
|
2.9
|
25.8
|
1.0
|
C1D
|
C:HEM602
|
2.9
|
25.8
|
1.0
|
C1A
|
C:HEM602
|
3.0
|
25.7
|
1.0
|
C4A
|
C:HEM602
|
3.1
|
26.0
|
1.0
|
C4C
|
C:HEM602
|
3.1
|
25.7
|
1.0
|
C4B
|
C:HEM602
|
3.1
|
25.8
|
1.0
|
C1B
|
C:HEM602
|
3.1
|
26.1
|
1.0
|
C1C
|
C:HEM602
|
3.1
|
25.5
|
1.0
|
CB
|
C:CYS429
|
3.3
|
27.4
|
1.0
|
CHA
|
C:HEM602
|
3.4
|
25.7
|
1.0
|
CHD
|
C:HEM602
|
3.4
|
25.7
|
1.0
|
CHB
|
C:HEM602
|
3.5
|
25.8
|
1.0
|
CHC
|
C:HEM602
|
3.5
|
25.5
|
1.0
|
CA
|
C:CYS429
|
4.0
|
28.1
|
1.0
|
C21
|
C:STR603
|
4.1
|
36.7
|
1.0
|
C3D
|
C:HEM602
|
4.2
|
25.8
|
1.0
|
C2D
|
C:HEM602
|
4.2
|
25.9
|
1.0
|
C2A
|
C:HEM602
|
4.2
|
26.3
|
1.0
|
C3A
|
C:HEM602
|
4.2
|
26.1
|
1.0
|
C3C
|
C:HEM602
|
4.3
|
25.6
|
1.0
|
C2C
|
C:HEM602
|
4.3
|
25.3
|
1.0
|
C2B
|
C:HEM602
|
4.3
|
26.0
|
1.0
|
C3B
|
C:HEM602
|
4.4
|
25.7
|
1.0
|
O
|
C:GLY292
|
4.7
|
32.4
|
1.0
|
N
|
C:LEU430
|
4.7
|
29.4
|
1.0
|
C
|
C:CYS429
|
4.7
|
28.9
|
1.0
|
CG2
|
C:THR296
|
4.9
|
37.0
|
1.0
|
C16
|
C:STR603
|
4.9
|
35.8
|
1.0
|
|
Reference:
P.S.Pallan,
C.Wang,
L.Lei,
F.K.Yoshimoto,
R.J.Auchus,
M.R.Waterman,
F.P.Guengerich,
M.Egli.
Human Cytochrome P450 21A2, the Major Steroid 21-Hydroxylase: Structure of the Enzyme-Progesterone Substrate Complex and Rate-Limiting C-H Bond Cleavage. J.Biol.Chem. 2015.
ISSN: ESSN 1083-351X
PubMed: 25855791
DOI: 10.1074/JBC.M115.646307
Page generated: Mon Aug 5 16:08:11 2024
|