Manganese in PDB 4pss: Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 100K
Protein crystallography data
The structure of Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 100K, PDB code: 4pss
was solved by
D.A.Keedy,
H.Van Den Bedem,
D.A.Sivak,
G.A.Petsko,
D.Ringe,
M.A.Wilson,
J.S.Fraser,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
40.78 /
0.85
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
33.960,
44.823,
98.254,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
15.3 /
16.9
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 100K
(pdb code 4pss). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the
Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 100K, PDB code: 4pss:
Jump to Manganese binding site number:
1;
2;
Manganese binding site 1 out
of 2 in 4pss
Go back to
Manganese Binding Sites List in 4pss
Manganese binding site 1 out
of 2 in the Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 100K
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 100K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn203
b:38.4
occ:1.00
|
ND1
|
A:HIS149
|
2.0
|
8.8
|
0.3
|
O
|
A:HOH588
|
2.0
|
21.1
|
1.0
|
O
|
A:ASP116
|
2.2
|
6.7
|
0.6
|
O
|
A:ASP116
|
2.2
|
6.7
|
0.4
|
O
|
A:HOH572
|
2.3
|
9.7
|
1.0
|
O
|
A:HOH573
|
2.5
|
34.6
|
1.0
|
ND1
|
A:HIS149
|
2.5
|
9.2
|
0.7
|
CE1
|
A:HIS149
|
2.6
|
9.4
|
0.3
|
HE1
|
A:HIS149
|
2.6
|
9.4
|
0.3
|
HA
|
A:ALA117
|
3.0
|
7.3
|
0.6
|
HA
|
A:ALA117
|
3.1
|
7.3
|
0.4
|
CG
|
A:HIS149
|
3.2
|
8.8
|
0.3
|
CE1
|
A:HIS149
|
3.3
|
10.5
|
0.7
|
C
|
A:ASP116
|
3.3
|
6.3
|
0.6
|
HE1
|
A:HIS149
|
3.4
|
9.4
|
0.7
|
C
|
A:ASP116
|
3.4
|
6.6
|
0.4
|
HA
|
A:HIS149
|
3.4
|
7.7
|
0.7
|
HB3
|
A:HIS149
|
3.5
|
8.9
|
0.7
|
CG
|
A:HIS149
|
3.5
|
7.9
|
0.7
|
HB3
|
A:HIS149
|
3.6
|
8.9
|
0.3
|
HA
|
A:HIS149
|
3.8
|
7.7
|
0.3
|
NE2
|
A:HIS149
|
3.8
|
9.7
|
0.3
|
HB2
|
A:ALA117
|
3.8
|
8.3
|
0.6
|
CB
|
A:HIS149
|
3.9
|
8.9
|
0.3
|
CB
|
A:HIS149
|
3.9
|
7.4
|
0.7
|
CA
|
A:ALA117
|
3.9
|
8.2
|
0.6
|
CA
|
A:ALA117
|
4.0
|
7.3
|
0.4
|
N
|
A:ALA117
|
4.0
|
6.8
|
0.6
|
O
|
A:HOH464
|
4.1
|
23.9
|
1.0
|
HB3
|
A:ASP116
|
4.1
|
6.9
|
0.6
|
HB2
|
A:ASP116
|
4.1
|
6.9
|
0.4
|
CD2
|
A:HIS149
|
4.1
|
9.6
|
0.3
|
N
|
A:ALA117
|
4.1
|
6.7
|
0.4
|
HB3
|
A:ASP116
|
4.2
|
6.9
|
0.4
|
CA
|
A:HIS149
|
4.2
|
6.3
|
0.7
|
HB2
|
A:ASP116
|
4.2
|
6.9
|
0.6
|
HB2
|
A:ALA117
|
4.3
|
8.3
|
0.4
|
H
|
A:SER150
|
4.3
|
7.1
|
0.7
|
CB
|
A:ALA117
|
4.4
|
8.7
|
0.6
|
H
|
A:SER150
|
4.4
|
7.1
|
0.3
|
CA
|
A:HIS149
|
4.4
|
7.7
|
0.3
|
NE2
|
A:HIS149
|
4.5
|
10.1
|
0.7
|
CB
|
A:ASP116
|
4.5
|
6.6
|
0.6
|
CA
|
A:ASP116
|
4.5
|
6.0
|
0.6
|
CB
|
A:ASP116
|
4.5
|
6.9
|
0.4
|
O
|
A:SER148
|
4.5
|
9.3
|
0.3
|
CA
|
A:ASP116
|
4.6
|
6.4
|
0.4
|
O
|
A:SER148
|
4.6
|
10.2
|
0.4
|
CD2
|
A:HIS149
|
4.6
|
9.7
|
0.7
|
HE2
|
A:HIS149
|
4.6
|
9.7
|
0.3
|
CB
|
A:ALA117
|
4.7
|
8.3
|
0.4
|
HB1
|
A:ALA117
|
4.7
|
8.3
|
0.6
|
H
|
A:GLU118
|
4.7
|
8.0
|
0.4
|
H
|
A:GLU118
|
4.8
|
8.0
|
0.6
|
O
|
A:HOH617
|
4.8
|
31.3
|
1.0
|
HB2
|
A:HIS149
|
4.9
|
8.9
|
0.3
|
HB2
|
A:HIS149
|
4.9
|
8.9
|
0.7
|
HB1
|
A:ALA117
|
5.0
|
8.3
|
0.4
|
|
Manganese binding site 2 out
of 2 in 4pss
Go back to
Manganese Binding Sites List in 4pss
Manganese binding site 2 out
of 2 in the Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 100K
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 100K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn204
b:33.1
occ:1.00
|
O
|
A:HOH566
|
2.1
|
15.2
|
1.0
|
O
|
A:HOH567
|
2.2
|
16.1
|
1.0
|
O
|
A:HOH570
|
2.2
|
15.7
|
1.0
|
O
|
A:HOH568
|
2.2
|
20.3
|
1.0
|
O
|
A:HOH569
|
2.2
|
14.6
|
1.0
|
OE2
|
A:GLU154
|
2.2
|
9.8
|
1.0
|
CD
|
A:GLU154
|
3.1
|
8.2
|
1.0
|
O
|
A:HOH344
|
3.2
|
11.4
|
1.0
|
HB2
|
A:SER135
|
3.3
|
10.2
|
1.0
|
OE1
|
A:GLU154
|
3.4
|
9.2
|
1.0
|
HG
|
A:SER135
|
3.5
|
9.7
|
1.0
|
HD21
|
A:LEU156
|
3.5
|
12.2
|
0.5
|
HD21
|
A:LEU156
|
3.9
|
12.2
|
0.5
|
CB
|
A:SER135
|
4.1
|
10.2
|
1.0
|
OG
|
A:SER135
|
4.2
|
9.7
|
1.0
|
O
|
A:HOH438
|
4.3
|
13.6
|
1.0
|
O
|
A:HOH561
|
4.4
|
12.9
|
1.0
|
HE2
|
A:HIS114
|
4.4
|
6.4
|
0.2
|
HB3
|
A:SER135
|
4.5
|
10.2
|
1.0
|
CD2
|
A:LEU156
|
4.5
|
9.3
|
0.5
|
CG
|
A:GLU154
|
4.5
|
9.2
|
1.0
|
O
|
A:HOH403
|
4.6
|
18.2
|
1.0
|
O
|
A:HOH354
|
4.6
|
18.5
|
1.0
|
HD23
|
A:LEU156
|
4.6
|
12.2
|
0.5
|
HE2
|
A:HIS114
|
4.6
|
6.4
|
0.2
|
HG3
|
A:GLU154
|
4.7
|
9.2
|
1.0
|
HE2
|
A:HIS114
|
4.7
|
6.4
|
0.3
|
HE2
|
A:HIS114
|
4.7
|
6.4
|
0.3
|
HD23
|
A:LEU156
|
4.8
|
12.2
|
0.5
|
CD2
|
A:LEU156
|
4.8
|
12.2
|
0.5
|
HD11
|
A:LEU156
|
5.0
|
14.0
|
0.5
|
|
Reference:
D.A.Keedy,
H.Van Den Bedem,
D.A.Sivak,
G.A.Petsko,
D.Ringe,
M.A.Wilson,
J.S.Fraser.
Crystal Cryocooling Distorts Conformational Heterogeneity in A Model Michaelis Complex of Dhfr. Structure V. 22 899 2014.
ISSN: ISSN 0969-2126
PubMed: 24882744
DOI: 10.1016/J.STR.2014.04.016
Page generated: Sat Oct 5 20:49:33 2024
|