Iron in PDB 4m11: Crystal Structure of Murine Cyclooxygenase-2 Complex with Meloxicam
Enzymatic activity of Crystal Structure of Murine Cyclooxygenase-2 Complex with Meloxicam
All present enzymatic activity of Crystal Structure of Murine Cyclooxygenase-2 Complex with Meloxicam:
1.14.99.1;
Protein crystallography data
The structure of Crystal Structure of Murine Cyclooxygenase-2 Complex with Meloxicam, PDB code: 4m11
was solved by
S.Xu,
S.Banerjee,
D.J.Hermanson,
L.J.Marnett,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
49.95 /
2.45
|
Space group
|
P 2 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
121.627,
133.538,
180.232,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20.2 /
23.1
|
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Murine Cyclooxygenase-2 Complex with Meloxicam
(pdb code 4m11). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Crystal Structure of Murine Cyclooxygenase-2 Complex with Meloxicam, PDB code: 4m11:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 4m11
Go back to
Iron Binding Sites List in 4m11
Iron binding site 1 out
of 4 in the Crystal Structure of Murine Cyclooxygenase-2 Complex with Meloxicam
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 Murine Cyclooxygenase-2 Complex with Meloxicam within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe605
b:25.6
occ:1.00
|
FE
|
A:HEM605
|
0.0
|
25.6
|
1.0
|
NA
|
A:HEM605
|
2.0
|
27.7
|
1.0
|
ND
|
A:HEM605
|
2.1
|
26.8
|
1.0
|
NB
|
A:HEM605
|
2.1
|
25.5
|
1.0
|
NC
|
A:HEM605
|
2.1
|
24.4
|
1.0
|
NE2
|
A:HIS388
|
2.3
|
33.8
|
1.0
|
O
|
A:HOH932
|
2.4
|
30.0
|
1.0
|
C1A
|
A:HEM605
|
3.0
|
29.0
|
1.0
|
C4D
|
A:HEM605
|
3.1
|
26.8
|
1.0
|
C4A
|
A:HEM605
|
3.1
|
28.1
|
1.0
|
C1D
|
A:HEM605
|
3.1
|
26.6
|
1.0
|
C1B
|
A:HEM605
|
3.1
|
26.1
|
1.0
|
C4B
|
A:HEM605
|
3.1
|
24.5
|
1.0
|
C1C
|
A:HEM605
|
3.1
|
24.1
|
1.0
|
C4C
|
A:HEM605
|
3.1
|
24.9
|
1.0
|
CD2
|
A:HIS388
|
3.1
|
34.5
|
1.0
|
CE1
|
A:HIS388
|
3.2
|
33.0
|
1.0
|
CHA
|
A:HEM605
|
3.4
|
27.6
|
1.0
|
CHD
|
A:HEM605
|
3.4
|
25.7
|
1.0
|
CHB
|
A:HEM605
|
3.5
|
27.4
|
1.0
|
CHC
|
A:HEM605
|
3.5
|
23.4
|
1.0
|
ND1
|
A:HIS388
|
4.2
|
33.7
|
1.0
|
CG
|
A:HIS388
|
4.3
|
34.7
|
1.0
|
C2A
|
A:HEM605
|
4.3
|
31.4
|
1.0
|
C3A
|
A:HEM605
|
4.3
|
29.4
|
1.0
|
C3D
|
A:HEM605
|
4.3
|
27.3
|
1.0
|
C2D
|
A:HEM605
|
4.3
|
27.3
|
1.0
|
C2B
|
A:HEM605
|
4.3
|
25.1
|
1.0
|
C3B
|
A:HEM605
|
4.3
|
25.1
|
1.0
|
C2C
|
A:HEM605
|
4.3
|
25.0
|
1.0
|
C3C
|
A:HEM605
|
4.3
|
26.1
|
1.0
|
NE2
|
A:GLN203
|
4.3
|
29.1
|
1.0
|
CE1
|
A:HIS207
|
4.5
|
28.1
|
1.0
|
NE2
|
A:HIS207
|
4.5
|
26.8
|
1.0
|
CD
|
A:GLN203
|
5.0
|
28.6
|
1.0
|
|
Iron binding site 2 out
of 4 in 4m11
Go back to
Iron Binding Sites List in 4m11
Iron binding site 2 out
of 4 in the Crystal Structure of Murine Cyclooxygenase-2 Complex with Meloxicam
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 Murine Cyclooxygenase-2 Complex with Meloxicam within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe605
b:30.3
occ:1.00
|
FE
|
B:HEM605
|
0.0
|
30.3
|
1.0
|
NA
|
B:HEM605
|
2.0
|
31.3
|
1.0
|
NC
|
B:HEM605
|
2.1
|
29.8
|
1.0
|
ND
|
B:HEM605
|
2.1
|
30.5
|
1.0
|
NB
|
B:HEM605
|
2.1
|
30.4
|
1.0
|
NE2
|
B:HIS388
|
2.3
|
39.4
|
1.0
|
O
|
B:HOH833
|
2.3
|
31.9
|
1.0
|
C1A
|
B:HEM605
|
3.0
|
32.1
|
1.0
|
C4A
|
B:HEM605
|
3.1
|
31.3
|
1.0
|
C1D
|
B:HEM605
|
3.1
|
30.2
|
1.0
|
C1C
|
B:HEM605
|
3.1
|
29.9
|
1.0
|
C4D
|
B:HEM605
|
3.1
|
29.8
|
1.0
|
C4C
|
B:HEM605
|
3.1
|
30.1
|
1.0
|
CD2
|
B:HIS388
|
3.1
|
39.4
|
1.0
|
C1B
|
B:HEM605
|
3.1
|
30.0
|
1.0
|
C4B
|
B:HEM605
|
3.1
|
29.8
|
1.0
|
CE1
|
B:HIS388
|
3.2
|
39.0
|
1.0
|
CHA
|
B:HEM605
|
3.4
|
30.4
|
1.0
|
CHD
|
B:HEM605
|
3.4
|
30.2
|
1.0
|
CHB
|
B:HEM605
|
3.5
|
30.1
|
1.0
|
CHC
|
B:HEM605
|
3.5
|
30.4
|
1.0
|
CG
|
B:HIS388
|
4.2
|
38.6
|
1.0
|
ND1
|
B:HIS388
|
4.2
|
39.2
|
1.0
|
C2A
|
B:HEM605
|
4.3
|
34.4
|
1.0
|
C3A
|
B:HEM605
|
4.3
|
32.1
|
1.0
|
C2C
|
B:HEM605
|
4.3
|
28.8
|
1.0
|
C2D
|
B:HEM605
|
4.3
|
30.0
|
1.0
|
C3C
|
B:HEM605
|
4.3
|
29.9
|
1.0
|
C3D
|
B:HEM605
|
4.3
|
29.5
|
1.0
|
C2B
|
B:HEM605
|
4.3
|
29.4
|
1.0
|
NE2
|
B:HIS207
|
4.3
|
33.3
|
1.0
|
C3B
|
B:HEM605
|
4.3
|
29.5
|
1.0
|
NE2
|
B:GLN203
|
4.3
|
30.7
|
1.0
|
O
|
B:HOH841
|
4.4
|
39.5
|
1.0
|
CE1
|
B:HIS207
|
4.8
|
32.9
|
1.0
|
|
Iron binding site 3 out
of 4 in 4m11
Go back to
Iron Binding Sites List in 4m11
Iron binding site 3 out
of 4 in the Crystal Structure of Murine Cyclooxygenase-2 Complex with Meloxicam
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 Murine Cyclooxygenase-2 Complex with Meloxicam within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe605
b:21.4
occ:1.00
|
FE
|
C:HEM605
|
0.0
|
21.4
|
1.0
|
NA
|
C:HEM605
|
2.0
|
22.0
|
1.0
|
NC
|
C:HEM605
|
2.1
|
17.6
|
1.0
|
NB
|
C:HEM605
|
2.1
|
23.7
|
1.0
|
ND
|
C:HEM605
|
2.1
|
19.8
|
1.0
|
NE2
|
C:HIS388
|
2.2
|
25.6
|
1.0
|
O
|
C:HOH849
|
2.9
|
39.3
|
1.0
|
C1A
|
C:HEM605
|
3.0
|
22.7
|
1.0
|
C4B
|
C:HEM605
|
3.1
|
22.9
|
1.0
|
C1C
|
C:HEM605
|
3.1
|
19.6
|
1.0
|
C4A
|
C:HEM605
|
3.1
|
23.1
|
1.0
|
C1B
|
C:HEM605
|
3.1
|
23.3
|
1.0
|
CD2
|
C:HIS388
|
3.1
|
26.7
|
1.0
|
C4D
|
C:HEM605
|
3.1
|
20.1
|
1.0
|
C4C
|
C:HEM605
|
3.1
|
18.5
|
1.0
|
C1D
|
C:HEM605
|
3.1
|
20.0
|
1.0
|
CE1
|
C:HIS388
|
3.3
|
26.4
|
1.0
|
CHC
|
C:HEM605
|
3.4
|
21.1
|
1.0
|
CHA
|
C:HEM605
|
3.4
|
20.8
|
1.0
|
CHB
|
C:HEM605
|
3.5
|
23.7
|
1.0
|
CHD
|
C:HEM605
|
3.5
|
20.4
|
1.0
|
CG
|
C:HIS388
|
4.3
|
27.4
|
1.0
|
C2A
|
C:HEM605
|
4.3
|
25.9
|
1.0
|
C3B
|
C:HEM605
|
4.3
|
23.9
|
1.0
|
C3A
|
C:HEM605
|
4.3
|
23.4
|
1.0
|
C2C
|
C:HEM605
|
4.3
|
19.1
|
1.0
|
C2B
|
C:HEM605
|
4.3
|
23.0
|
1.0
|
ND1
|
C:HIS388
|
4.3
|
26.5
|
1.0
|
C3C
|
C:HEM605
|
4.3
|
18.6
|
1.0
|
C3D
|
C:HEM605
|
4.3
|
20.7
|
1.0
|
NE2
|
C:GLN203
|
4.3
|
20.1
|
1.0
|
C2D
|
C:HEM605
|
4.3
|
20.0
|
1.0
|
NE2
|
C:HIS207
|
4.5
|
24.2
|
1.0
|
CE1
|
C:HIS207
|
4.7
|
24.4
|
1.0
|
O
|
C:HOH904
|
4.9
|
46.1
|
1.0
|
CD
|
C:GLN203
|
5.0
|
20.2
|
1.0
|
|
Iron binding site 4 out
of 4 in 4m11
Go back to
Iron Binding Sites List in 4m11
Iron binding site 4 out
of 4 in the Crystal Structure of Murine Cyclooxygenase-2 Complex with Meloxicam
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Crystal Structure of Murine Cyclooxygenase-2 Complex with Meloxicam within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe605
b:24.0
occ:1.00
|
FE
|
D:HEM605
|
0.0
|
24.0
|
1.0
|
NC
|
D:HEM605
|
2.0
|
22.7
|
1.0
|
NA
|
D:HEM605
|
2.1
|
29.5
|
1.0
|
NB
|
D:HEM605
|
2.1
|
26.8
|
1.0
|
ND
|
D:HEM605
|
2.1
|
25.8
|
1.0
|
NE2
|
D:HIS388
|
2.3
|
25.9
|
1.0
|
O
|
D:HOH911
|
2.6
|
25.2
|
1.0
|
C1C
|
D:HEM605
|
3.0
|
22.9
|
1.0
|
C4B
|
D:HEM605
|
3.1
|
26.0
|
1.0
|
C1A
|
D:HEM605
|
3.1
|
30.5
|
1.0
|
C4A
|
D:HEM605
|
3.1
|
29.1
|
1.0
|
C4C
|
D:HEM605
|
3.1
|
22.4
|
1.0
|
C4D
|
D:HEM605
|
3.1
|
26.2
|
1.0
|
C1B
|
D:HEM605
|
3.1
|
26.2
|
1.0
|
C1D
|
D:HEM605
|
3.1
|
24.6
|
1.0
|
CD2
|
D:HIS388
|
3.1
|
25.4
|
1.0
|
CE1
|
D:HIS388
|
3.3
|
25.6
|
1.0
|
CHC
|
D:HEM605
|
3.4
|
24.8
|
1.0
|
CHA
|
D:HEM605
|
3.4
|
28.3
|
1.0
|
CHD
|
D:HEM605
|
3.5
|
23.4
|
1.0
|
CHB
|
D:HEM605
|
3.5
|
27.5
|
1.0
|
NE2
|
D:GLN203
|
4.0
|
22.1
|
1.0
|
C2C
|
D:HEM605
|
4.3
|
21.3
|
1.0
|
C3B
|
D:HEM605
|
4.3
|
25.3
|
1.0
|
C2A
|
D:HEM605
|
4.3
|
33.1
|
1.0
|
C2B
|
D:HEM605
|
4.3
|
24.8
|
1.0
|
CG
|
D:HIS388
|
4.3
|
25.2
|
1.0
|
C3A
|
D:HEM605
|
4.3
|
30.8
|
1.0
|
C3C
|
D:HEM605
|
4.3
|
21.8
|
1.0
|
C2D
|
D:HEM605
|
4.3
|
24.8
|
1.0
|
C3D
|
D:HEM605
|
4.3
|
25.1
|
1.0
|
ND1
|
D:HIS388
|
4.3
|
25.2
|
1.0
|
NE2
|
D:HIS207
|
4.4
|
26.9
|
1.0
|
CE1
|
D:HIS207
|
4.6
|
25.4
|
1.0
|
CD
|
D:GLN203
|
4.8
|
21.7
|
1.0
|
CG
|
D:GLN203
|
4.9
|
20.0
|
1.0
|
|
Reference:
S.Xu,
D.J.Hermanson,
S.Banerjee,
K.Ghebreselasie,
G.M.Clayton,
R.M.Garavito,
L.J.Marnett.
Oxicams Bind in A Novel Mode to the Cyclooxygenase Active Site Via A Two-Water-Mediated H-Bonding Network. J.Biol.Chem. V. 289 6799 2014.
ISSN: ISSN 0021-9258
PubMed: 24425867
DOI: 10.1074/JBC.M113.517987
Page generated: Mon Aug 5 06:33:29 2024
|