Manganese in PDB 6ds8: Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site
Enzymatic activity of Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site
All present enzymatic activity of Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site:
1.14.14.18;
Protein crystallography data
The structure of Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site, PDB code: 6ds8
was solved by
A.Chao,
C.W.Goulding,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.50 /
2.40
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
39.020,
68.701,
74.490,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
18.1 /
24.2
|
Other elements in 6ds8:
The structure of Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site
(pdb code 6ds8). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the
Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site, PDB code: 6ds8:
Jump to Manganese binding site number:
1;
2;
3;
4;
Manganese binding site 1 out
of 4 in 6ds8
Go back to
Manganese Binding Sites List in 6ds8
Manganese binding site 1 out
of 4 in the Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn201
b:30.4
occ:1.00
|
MN
|
A:MNH201
|
0.0
|
30.4
|
1.0
|
NA
|
A:MNH201
|
2.1
|
28.6
|
1.0
|
ND
|
A:MNH201
|
2.1
|
25.0
|
1.0
|
NC
|
A:MNH201
|
2.1
|
22.0
|
1.0
|
NB
|
A:MNH201
|
2.2
|
25.7
|
1.0
|
NE2
|
A:HIS75
|
2.5
|
33.2
|
1.0
|
C1A
|
A:MNH201
|
3.0
|
30.2
|
1.0
|
C4A
|
A:MNH201
|
3.0
|
31.9
|
1.0
|
CHD
|
A:MNH201
|
3.1
|
27.3
|
1.0
|
C4D
|
A:MNH201
|
3.1
|
29.5
|
1.0
|
C1D
|
A:MNH201
|
3.1
|
27.2
|
1.0
|
C4C
|
A:MNH201
|
3.1
|
26.3
|
1.0
|
CHA
|
A:MNH201
|
3.1
|
31.1
|
1.0
|
CHB
|
A:MNH201
|
3.1
|
28.6
|
1.0
|
C1B
|
A:MNH201
|
3.2
|
25.4
|
1.0
|
C1C
|
A:MNH201
|
3.2
|
24.6
|
1.0
|
C4B
|
A:MNH201
|
3.2
|
27.8
|
1.0
|
C4D
|
A:MNH202
|
3.3
|
27.2
|
1.0
|
CHA
|
A:MNH202
|
3.3
|
20.6
|
1.0
|
CHC
|
A:MNH201
|
3.3
|
27.4
|
1.0
|
CE1
|
A:HIS75
|
3.3
|
34.0
|
1.0
|
CD2
|
A:HIS75
|
3.6
|
29.5
|
1.0
|
ND
|
A:MNH202
|
3.6
|
25.1
|
1.0
|
C1A
|
A:MNH202
|
3.7
|
25.1
|
1.0
|
C3D
|
A:MNH202
|
3.8
|
28.8
|
1.0
|
NA
|
A:MNH202
|
4.0
|
23.6
|
1.0
|
C2A
|
A:MNH201
|
4.2
|
28.6
|
1.0
|
C3A
|
A:MNH201
|
4.2
|
34.5
|
1.0
|
C1D
|
A:MNH202
|
4.2
|
25.8
|
1.0
|
C3D
|
A:MNH201
|
4.3
|
31.2
|
1.0
|
C2D
|
A:MNH201
|
4.3
|
30.7
|
1.0
|
C3C
|
A:MNH201
|
4.3
|
20.9
|
1.0
|
C3B
|
A:MNH201
|
4.3
|
23.2
|
1.0
|
C2C
|
A:MNH201
|
4.4
|
21.9
|
1.0
|
C2B
|
A:MNH201
|
4.4
|
29.5
|
1.0
|
C2D
|
A:MNH202
|
4.5
|
23.4
|
1.0
|
ND1
|
A:HIS75
|
4.5
|
31.1
|
1.0
|
CAD
|
A:MNH202
|
4.5
|
30.1
|
1.0
|
C2A
|
A:MNH202
|
4.6
|
26.8
|
1.0
|
MN
|
A:MNH202
|
4.6
|
25.7
|
1.0
|
CG
|
A:HIS75
|
4.7
|
31.5
|
1.0
|
C4A
|
A:MNH202
|
4.8
|
25.4
|
1.0
|
CHD
|
A:MNH202
|
5.0
|
22.1
|
1.0
|
|
Manganese binding site 2 out
of 4 in 6ds8
Go back to
Manganese Binding Sites List in 6ds8
Manganese binding site 2 out
of 4 in the Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn202
b:25.7
occ:1.00
|
MN
|
A:MNH202
|
0.0
|
25.7
|
1.0
|
ND
|
A:MNH202
|
2.1
|
25.1
|
1.0
|
NA
|
A:MNH202
|
2.1
|
23.6
|
1.0
|
NC
|
A:MNH202
|
2.1
|
23.5
|
1.0
|
NB
|
A:MNH202
|
2.2
|
22.2
|
1.0
|
CL
|
A:CL203
|
2.5
|
25.1
|
1.0
|
C4D
|
A:MNH202
|
3.1
|
27.2
|
1.0
|
C1D
|
A:MNH202
|
3.1
|
25.8
|
1.0
|
CHD
|
A:MNH202
|
3.1
|
22.1
|
1.0
|
C4C
|
A:MNH202
|
3.1
|
26.9
|
1.0
|
C1A
|
A:MNH202
|
3.1
|
25.1
|
1.0
|
C4B
|
A:MNH202
|
3.2
|
25.4
|
1.0
|
C1C
|
A:MNH202
|
3.2
|
25.3
|
1.0
|
C4A
|
A:MNH202
|
3.2
|
25.4
|
1.0
|
CHA
|
A:MNH202
|
3.2
|
20.6
|
1.0
|
C1B
|
A:MNH202
|
3.3
|
23.9
|
1.0
|
CHC
|
A:MNH202
|
3.3
|
23.6
|
1.0
|
CHB
|
A:MNH202
|
3.4
|
21.7
|
1.0
|
C4C
|
A:MNH201
|
3.6
|
26.3
|
1.0
|
CHD
|
A:MNH201
|
3.7
|
27.3
|
1.0
|
NC
|
A:MNH201
|
4.0
|
22.0
|
1.0
|
C3C
|
A:MNH201
|
4.0
|
20.9
|
1.0
|
C3D
|
A:MNH202
|
4.3
|
28.8
|
1.0
|
ND2
|
A:ASN7
|
4.3
|
25.1
|
1.0
|
C1D
|
A:MNH201
|
4.3
|
27.2
|
1.0
|
C3B
|
A:MNH202
|
4.4
|
29.4
|
1.0
|
C2A
|
A:MNH202
|
4.4
|
26.8
|
1.0
|
C3C
|
A:MNH202
|
4.4
|
23.4
|
1.0
|
C2D
|
A:MNH202
|
4.4
|
23.4
|
1.0
|
C2C
|
A:MNH202
|
4.4
|
22.1
|
1.0
|
CAC
|
A:MNH201
|
4.4
|
23.3
|
1.0
|
C3A
|
A:MNH202
|
4.5
|
24.9
|
1.0
|
C1C
|
A:MNH201
|
4.5
|
24.6
|
1.0
|
C2C
|
A:MNH201
|
4.5
|
21.9
|
1.0
|
C2B
|
A:MNH202
|
4.6
|
29.4
|
1.0
|
CZ
|
A:PHE23
|
4.6
|
20.2
|
1.0
|
MN
|
A:MNH201
|
4.6
|
30.4
|
1.0
|
ND
|
A:MNH201
|
4.6
|
25.0
|
1.0
|
|
Manganese binding site 3 out
of 4 in 6ds8
Go back to
Manganese Binding Sites List in 6ds8
Manganese binding site 3 out
of 4 in the Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn201
b:30.2
occ:1.00
|
MN
|
B:MNH201
|
0.0
|
30.2
|
1.0
|
ND
|
B:MNH201
|
2.1
|
23.8
|
1.0
|
NA
|
B:MNH201
|
2.1
|
30.1
|
1.0
|
NC
|
B:MNH201
|
2.2
|
28.5
|
1.0
|
NB
|
B:MNH201
|
2.2
|
26.1
|
1.0
|
NE2
|
B:HIS75
|
2.4
|
26.7
|
1.0
|
C1A
|
B:MNH201
|
3.1
|
26.0
|
1.0
|
C4D
|
B:MNH201
|
3.1
|
27.0
|
1.0
|
C4C
|
B:MNH201
|
3.2
|
26.7
|
1.0
|
CHA
|
B:MNH201
|
3.2
|
26.0
|
1.0
|
C1D
|
B:MNH201
|
3.2
|
26.6
|
1.0
|
C4B
|
B:MNH201
|
3.2
|
29.3
|
1.0
|
C1C
|
B:MNH201
|
3.2
|
27.3
|
1.0
|
C4A
|
B:MNH201
|
3.2
|
32.0
|
1.0
|
CHD
|
B:MNH201
|
3.2
|
22.1
|
1.0
|
CE1
|
B:HIS75
|
3.2
|
23.8
|
1.0
|
C1B
|
B:MNH201
|
3.2
|
32.1
|
1.0
|
CHC
|
B:MNH201
|
3.3
|
25.7
|
1.0
|
CHB
|
B:MNH201
|
3.3
|
29.2
|
1.0
|
CHA
|
B:MNH202
|
3.4
|
24.5
|
1.0
|
C4D
|
B:MNH202
|
3.4
|
23.1
|
1.0
|
CD2
|
B:HIS75
|
3.5
|
23.7
|
1.0
|
C1A
|
B:MNH202
|
3.8
|
27.1
|
1.0
|
ND
|
B:MNH202
|
3.8
|
19.9
|
1.0
|
C3D
|
B:MNH202
|
3.9
|
26.5
|
1.0
|
NA
|
B:MNH202
|
4.1
|
25.5
|
1.0
|
C3D
|
B:MNH201
|
4.3
|
27.3
|
1.0
|
C2A
|
B:MNH201
|
4.4
|
30.0
|
1.0
|
C3B
|
B:MNH201
|
4.4
|
30.6
|
1.0
|
C3C
|
B:MNH201
|
4.4
|
25.5
|
1.0
|
ND1
|
B:HIS75
|
4.4
|
25.4
|
1.0
|
C1D
|
B:MNH202
|
4.4
|
24.5
|
1.0
|
C2C
|
B:MNH201
|
4.4
|
26.9
|
1.0
|
C2D
|
B:MNH201
|
4.5
|
27.8
|
1.0
|
C3A
|
B:MNH201
|
4.5
|
30.0
|
1.0
|
CAD
|
B:MNH202
|
4.5
|
31.1
|
1.0
|
C2B
|
B:MNH201
|
4.5
|
35.6
|
1.0
|
C2A
|
B:MNH202
|
4.5
|
26.0
|
1.0
|
CG
|
B:HIS75
|
4.6
|
26.2
|
1.0
|
C2D
|
B:MNH202
|
4.6
|
27.1
|
1.0
|
MN
|
B:MNH202
|
4.8
|
26.3
|
1.0
|
C4A
|
B:MNH202
|
4.9
|
28.5
|
1.0
|
CAA
|
B:MNH202
|
5.0
|
33.4
|
1.0
|
|
Manganese binding site 4 out
of 4 in 6ds8
Go back to
Manganese Binding Sites List in 6ds8
Manganese binding site 4 out
of 4 in the Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn202
b:26.3
occ:1.00
|
MN
|
B:MNH202
|
0.0
|
26.3
|
1.0
|
ND
|
B:MNH202
|
2.1
|
19.9
|
1.0
|
NA
|
B:MNH202
|
2.1
|
25.5
|
1.0
|
NC
|
B:MNH202
|
2.1
|
20.9
|
1.0
|
NB
|
B:MNH202
|
2.2
|
23.2
|
1.0
|
CL
|
B:CL203
|
2.5
|
25.7
|
1.0
|
C4C
|
B:MNH202
|
3.1
|
23.3
|
1.0
|
C1D
|
B:MNH202
|
3.1
|
24.5
|
1.0
|
CHD
|
B:MNH202
|
3.1
|
21.9
|
1.0
|
C4D
|
B:MNH202
|
3.1
|
23.1
|
1.0
|
C1A
|
B:MNH202
|
3.1
|
27.1
|
1.0
|
C4A
|
B:MNH202
|
3.2
|
28.5
|
1.0
|
C1C
|
B:MNH202
|
3.2
|
26.4
|
1.0
|
C4B
|
B:MNH202
|
3.2
|
24.9
|
1.0
|
CHA
|
B:MNH202
|
3.3
|
24.5
|
1.0
|
C1B
|
B:MNH202
|
3.3
|
26.4
|
1.0
|
CHB
|
B:MNH202
|
3.3
|
24.9
|
1.0
|
CHC
|
B:MNH202
|
3.3
|
21.9
|
1.0
|
C4C
|
B:MNH201
|
3.8
|
26.7
|
1.0
|
ND2
|
B:ASN7
|
3.9
|
22.3
|
1.0
|
CHD
|
B:MNH201
|
3.9
|
22.1
|
1.0
|
C3C
|
B:MNH201
|
4.2
|
25.5
|
1.0
|
NC
|
B:MNH201
|
4.2
|
28.5
|
1.0
|
C3D
|
B:MNH202
|
4.3
|
26.5
|
1.0
|
C3C
|
B:MNH202
|
4.4
|
23.8
|
1.0
|
C2A
|
B:MNH202
|
4.4
|
26.0
|
1.0
|
C3B
|
B:MNH202
|
4.4
|
27.1
|
1.0
|
C2D
|
B:MNH202
|
4.4
|
27.1
|
1.0
|
C2C
|
B:MNH202
|
4.4
|
24.0
|
1.0
|
C3A
|
B:MNH202
|
4.5
|
27.5
|
1.0
|
C1D
|
B:MNH201
|
4.5
|
26.6
|
1.0
|
C2B
|
B:MNH202
|
4.5
|
26.9
|
1.0
|
CAC
|
B:MNH201
|
4.6
|
24.3
|
1.0
|
CZ
|
B:PHE23
|
4.7
|
21.8
|
1.0
|
C1C
|
B:MNH201
|
4.7
|
27.3
|
1.0
|
C2C
|
B:MNH201
|
4.7
|
26.9
|
1.0
|
ND
|
B:MNH201
|
4.8
|
23.8
|
1.0
|
MN
|
B:MNH201
|
4.8
|
30.2
|
1.0
|
CG
|
B:ASN7
|
4.9
|
24.1
|
1.0
|
|
Reference:
A.Chao,
C.W.Goulding.
Crystal Structure of Mhud R26S Mutant with Two Manganese Protoporphyrin IX Bound Per Active Site To Be Published.
Page generated: Sun Oct 6 04:12:14 2024
|