Manganese in PDB 1g5b: Bacteriophage Lambda Ser/Thr Protein Phosphatase
Protein crystallography data
The structure of Bacteriophage Lambda Ser/Thr Protein Phosphatase, PDB code: 1g5b
was solved by
W.C.Voegtli,
D.J.White,
N.J.Reiter,
F.Rusnak,
A.C.Rosenzweig,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
35.00 /
2.15
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
160.400,
177.300,
79.100,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20 /
22.6
|
Other elements in 1g5b:
The structure of Bacteriophage Lambda Ser/Thr Protein Phosphatase also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Bacteriophage Lambda Ser/Thr Protein Phosphatase
(pdb code 1g5b). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the
Bacteriophage Lambda Ser/Thr Protein Phosphatase, PDB code: 1g5b:
Jump to Manganese binding site number:
1;
2;
3;
4;
5;
6;
Manganese binding site 1 out
of 6 in 1g5b
Go back to
Manganese Binding Sites List in 1g5b
Manganese binding site 1 out
of 6 in the Bacteriophage Lambda Ser/Thr Protein Phosphatase
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Bacteriophage Lambda Ser/Thr Protein Phosphatase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn1005
b:31.6
occ:1.00
|
OD1
|
A:ASN75
|
2.1
|
26.4
|
1.0
|
NE2
|
A:HIS139
|
2.2
|
33.7
|
1.0
|
ND1
|
A:HIS186
|
2.2
|
29.9
|
1.0
|
O
|
A:HOH3056
|
2.3
|
34.6
|
1.0
|
OD2
|
A:ASP49
|
2.3
|
26.9
|
1.0
|
O3
|
A:SO43001
|
2.4
|
46.7
|
1.0
|
CE1
|
A:HIS186
|
3.0
|
26.7
|
1.0
|
CE1
|
A:HIS139
|
3.1
|
31.3
|
1.0
|
CG
|
A:ASP49
|
3.2
|
26.5
|
1.0
|
CG
|
A:ASN75
|
3.2
|
27.3
|
1.0
|
CD2
|
A:HIS139
|
3.2
|
36.4
|
1.0
|
CG
|
A:HIS186
|
3.4
|
29.6
|
1.0
|
OD1
|
A:ASP49
|
3.4
|
29.7
|
1.0
|
MN
|
A:MN1006
|
3.5
|
38.0
|
1.0
|
S
|
A:SO43001
|
3.6
|
48.2
|
1.0
|
CA
|
A:HIS186
|
3.7
|
36.6
|
1.0
|
ND2
|
A:ASN75
|
3.7
|
29.8
|
1.0
|
O1
|
A:SO43001
|
3.8
|
42.5
|
1.0
|
CB
|
A:HIS186
|
3.8
|
30.3
|
1.0
|
OD2
|
A:ASP20
|
4.0
|
34.1
|
1.0
|
CD2
|
A:HIS76
|
4.0
|
25.2
|
1.0
|
NE2
|
A:HIS186
|
4.2
|
33.7
|
1.0
|
ND1
|
A:HIS139
|
4.2
|
34.0
|
1.0
|
O
|
A:HIS186
|
4.3
|
38.7
|
1.0
|
CG
|
A:HIS139
|
4.3
|
38.2
|
1.0
|
CD2
|
A:HIS186
|
4.4
|
29.8
|
1.0
|
O2
|
A:SO43001
|
4.4
|
46.3
|
1.0
|
CB
|
A:ASP49
|
4.5
|
24.4
|
1.0
|
O
|
A:HOH3047
|
4.5
|
38.0
|
1.0
|
N
|
A:ASN75
|
4.5
|
30.7
|
1.0
|
CB
|
A:ASN75
|
4.5
|
27.0
|
1.0
|
C
|
A:HIS186
|
4.5
|
37.9
|
1.0
|
O
|
A:ILE159
|
4.6
|
36.7
|
1.0
|
NE2
|
A:HIS76
|
4.7
|
29.0
|
1.0
|
O4
|
A:SO43001
|
4.7
|
46.9
|
1.0
|
N
|
A:HIS186
|
4.7
|
33.6
|
1.0
|
|
Manganese binding site 2 out
of 6 in 1g5b
Go back to
Manganese Binding Sites List in 1g5b
Manganese binding site 2 out
of 6 in the Bacteriophage Lambda Ser/Thr Protein Phosphatase
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Bacteriophage Lambda Ser/Thr Protein Phosphatase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn1006
b:38.0
occ:1.00
|
O
|
A:HOH3056
|
2.1
|
34.6
|
1.0
|
NE2
|
A:HIS22
|
2.2
|
27.5
|
1.0
|
OD2
|
A:ASP49
|
2.2
|
26.9
|
1.0
|
O
|
A:HOH3055
|
2.3
|
36.2
|
1.0
|
OD2
|
A:ASP20
|
2.4
|
34.1
|
1.0
|
O
|
A:HOH3047
|
2.6
|
38.0
|
1.0
|
CE1
|
A:HIS22
|
3.1
|
29.1
|
1.0
|
CG
|
A:ASP49
|
3.2
|
26.5
|
1.0
|
CD2
|
A:HIS22
|
3.3
|
28.0
|
1.0
|
CG
|
A:ASP20
|
3.3
|
35.1
|
1.0
|
MN
|
A:MN1005
|
3.5
|
31.6
|
1.0
|
CB
|
A:ASP49
|
3.6
|
24.4
|
1.0
|
CB
|
A:ASP20
|
3.7
|
30.9
|
1.0
|
O3
|
A:SO43001
|
4.0
|
46.7
|
1.0
|
OD2
|
A:ASP202
|
4.2
|
33.3
|
1.0
|
ND1
|
A:HIS22
|
4.2
|
27.2
|
1.0
|
O1
|
A:SO43001
|
4.3
|
42.5
|
1.0
|
O
|
A:HIS186
|
4.3
|
38.7
|
1.0
|
OD1
|
A:ASP49
|
4.4
|
29.7
|
1.0
|
CG
|
A:HIS22
|
4.4
|
29.2
|
1.0
|
CE1
|
A:HIS139
|
4.4
|
31.3
|
1.0
|
CD2
|
A:HIS76
|
4.4
|
25.2
|
1.0
|
OD1
|
A:ASP20
|
4.5
|
34.6
|
1.0
|
O
|
A:HOH3021
|
4.5
|
40.2
|
1.0
|
CA
|
A:HIS186
|
4.5
|
36.6
|
1.0
|
NE2
|
A:HIS139
|
4.6
|
33.7
|
1.0
|
NE2
|
A:HIS76
|
4.6
|
29.0
|
1.0
|
S
|
A:SO43001
|
4.6
|
48.2
|
1.0
|
C
|
A:HIS186
|
4.8
|
37.9
|
1.0
|
O4
|
A:SO43001
|
4.9
|
46.9
|
1.0
|
N
|
A:HIS186
|
4.9
|
33.6
|
1.0
|
|
Manganese binding site 3 out
of 6 in 1g5b
Go back to
Manganese Binding Sites List in 1g5b
Manganese binding site 3 out
of 6 in the Bacteriophage Lambda Ser/Thr Protein Phosphatase
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Bacteriophage Lambda Ser/Thr Protein Phosphatase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn1003
b:27.4
occ:1.00
|
OD2
|
B:ASP20
|
2.2
|
26.5
|
1.0
|
OD2
|
B:ASP49
|
2.2
|
32.4
|
1.0
|
NE2
|
B:HIS22
|
2.2
|
21.4
|
1.0
|
O
|
B:HOH3011
|
2.2
|
26.0
|
1.0
|
O
|
B:HOH3012
|
2.3
|
29.5
|
1.0
|
O
|
B:HOH3088
|
2.4
|
42.7
|
1.0
|
CE1
|
B:HIS22
|
3.2
|
23.1
|
1.0
|
CG
|
B:ASP20
|
3.2
|
25.0
|
1.0
|
CD2
|
B:HIS22
|
3.2
|
21.5
|
1.0
|
CG
|
B:ASP49
|
3.2
|
30.8
|
1.0
|
MN
|
B:MN1004
|
3.5
|
26.9
|
1.0
|
CB
|
B:ASP49
|
3.6
|
25.9
|
1.0
|
CB
|
B:ASP20
|
3.7
|
24.7
|
1.0
|
O
|
B:HOH3074
|
3.8
|
46.3
|
1.0
|
O2
|
B:SO43002
|
3.9
|
35.4
|
1.0
|
OD2
|
B:ASP202
|
4.2
|
29.3
|
1.0
|
O
|
B:HIS186
|
4.2
|
25.3
|
1.0
|
O4
|
B:SO43002
|
4.2
|
40.0
|
1.0
|
OD1
|
B:ASP20
|
4.3
|
22.8
|
1.0
|
ND1
|
B:HIS22
|
4.3
|
23.1
|
1.0
|
OD1
|
B:ASP49
|
4.4
|
30.6
|
1.0
|
CG
|
B:HIS22
|
4.4
|
25.4
|
1.0
|
CE1
|
B:HIS139
|
4.4
|
27.1
|
1.0
|
CD2
|
B:HIS76
|
4.4
|
25.2
|
1.0
|
CA
|
B:HIS186
|
4.4
|
26.3
|
1.0
|
O
|
B:HOH3008
|
4.5
|
29.1
|
1.0
|
NE2
|
B:HIS139
|
4.6
|
25.5
|
1.0
|
S
|
B:SO43002
|
4.6
|
38.7
|
1.0
|
NE2
|
B:HIS76
|
4.7
|
28.3
|
1.0
|
C
|
B:HIS186
|
4.7
|
27.0
|
1.0
|
ND1
|
B:HIS186
|
4.9
|
25.3
|
1.0
|
N
|
B:HIS186
|
4.9
|
25.8
|
1.0
|
|
Manganese binding site 4 out
of 6 in 1g5b
Go back to
Manganese Binding Sites List in 1g5b
Manganese binding site 4 out
of 6 in the Bacteriophage Lambda Ser/Thr Protein Phosphatase
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Bacteriophage Lambda Ser/Thr Protein Phosphatase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn1004
b:26.9
occ:1.00
|
OD1
|
B:ASN75
|
2.2
|
25.8
|
1.0
|
NE2
|
B:HIS139
|
2.2
|
25.5
|
1.0
|
ND1
|
B:HIS186
|
2.2
|
25.3
|
1.0
|
O2
|
B:SO43002
|
2.3
|
35.4
|
1.0
|
O
|
B:HOH3011
|
2.4
|
26.0
|
1.0
|
OD2
|
B:ASP49
|
2.4
|
32.4
|
1.0
|
CE1
|
B:HIS186
|
3.0
|
23.8
|
1.0
|
CE1
|
B:HIS139
|
3.1
|
27.1
|
1.0
|
CG
|
B:ASN75
|
3.2
|
27.9
|
1.0
|
CG
|
B:ASP49
|
3.2
|
30.8
|
1.0
|
CD2
|
B:HIS139
|
3.3
|
25.8
|
1.0
|
CG
|
B:HIS186
|
3.4
|
26.6
|
1.0
|
OD1
|
B:ASP49
|
3.4
|
30.6
|
1.0
|
MN
|
B:MN1003
|
3.5
|
27.4
|
1.0
|
ND2
|
B:ASN75
|
3.6
|
24.3
|
1.0
|
S
|
B:SO43002
|
3.6
|
38.7
|
1.0
|
CA
|
B:HIS186
|
3.8
|
26.3
|
1.0
|
CB
|
B:HIS186
|
3.8
|
25.4
|
1.0
|
O4
|
B:SO43002
|
3.9
|
40.0
|
1.0
|
OD2
|
B:ASP20
|
3.9
|
26.5
|
1.0
|
O
|
B:HOH3088
|
4.1
|
42.7
|
1.0
|
CD2
|
B:HIS76
|
4.1
|
25.2
|
1.0
|
NE2
|
B:HIS186
|
4.2
|
30.0
|
1.0
|
O
|
B:HIS186
|
4.3
|
25.3
|
1.0
|
ND1
|
B:HIS139
|
4.3
|
26.4
|
1.0
|
O3
|
B:SO43002
|
4.3
|
41.3
|
1.0
|
CG
|
B:HIS139
|
4.4
|
29.5
|
1.0
|
CD2
|
B:HIS186
|
4.4
|
28.3
|
1.0
|
CB
|
B:ASN75
|
4.5
|
25.3
|
1.0
|
CB
|
B:ASP49
|
4.5
|
25.9
|
1.0
|
O
|
B:ILE159
|
4.5
|
31.4
|
1.0
|
C
|
B:HIS186
|
4.5
|
27.0
|
1.0
|
N
|
B:ASN75
|
4.6
|
25.4
|
1.0
|
O1
|
B:SO43002
|
4.7
|
41.6
|
1.0
|
NE2
|
B:HIS76
|
4.7
|
28.3
|
1.0
|
N
|
B:HIS186
|
4.8
|
25.8
|
1.0
|
|
Manganese binding site 5 out
of 6 in 1g5b
Go back to
Manganese Binding Sites List in 1g5b
Manganese binding site 5 out
of 6 in the Bacteriophage Lambda Ser/Thr Protein Phosphatase
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 5 of Bacteriophage Lambda Ser/Thr Protein Phosphatase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn1001
b:28.6
occ:1.00
|
O1
|
C:SO43003
|
2.1
|
33.9
|
1.0
|
NE2
|
C:HIS22
|
2.2
|
22.2
|
1.0
|
OD2
|
C:ASP20
|
2.2
|
29.6
|
1.0
|
O
|
C:HOH3082
|
2.2
|
23.8
|
1.0
|
OD2
|
C:ASP49
|
2.4
|
26.1
|
1.0
|
O3
|
C:SO43003
|
2.6
|
31.6
|
1.0
|
S
|
C:SO43003
|
2.9
|
34.9
|
1.0
|
CE1
|
C:HIS22
|
3.1
|
25.0
|
1.0
|
CD2
|
C:HIS22
|
3.2
|
22.6
|
1.0
|
CG
|
C:ASP20
|
3.2
|
33.5
|
1.0
|
CG
|
C:ASP49
|
3.3
|
26.3
|
1.0
|
MN
|
C:MN1002
|
3.4
|
26.6
|
1.0
|
CB
|
C:ASP49
|
3.6
|
24.7
|
1.0
|
CB
|
C:ASP20
|
3.6
|
29.8
|
1.0
|
O2
|
C:SO43003
|
3.8
|
31.4
|
1.0
|
O4
|
C:SO43003
|
4.0
|
25.8
|
1.0
|
O
|
C:HOH3019
|
4.1
|
32.2
|
1.0
|
OD2
|
C:ASP202
|
4.1
|
29.7
|
1.0
|
ND1
|
C:HIS22
|
4.2
|
26.2
|
1.0
|
CG
|
C:HIS22
|
4.3
|
22.1
|
1.0
|
OD1
|
C:ASP20
|
4.3
|
31.5
|
1.0
|
CE1
|
C:HIS139
|
4.3
|
25.2
|
1.0
|
O
|
C:HIS186
|
4.4
|
37.6
|
1.0
|
CA
|
C:HIS186
|
4.5
|
29.7
|
1.0
|
OD1
|
C:ASP49
|
4.5
|
28.4
|
1.0
|
O
|
C:HOH3020
|
4.6
|
35.7
|
1.0
|
NE2
|
C:HIS139
|
4.6
|
27.7
|
1.0
|
CD2
|
C:HIS76
|
4.6
|
26.2
|
1.0
|
NE
|
C:ARG53
|
4.6
|
33.3
|
1.0
|
N
|
C:HIS186
|
4.8
|
31.3
|
1.0
|
C
|
C:HIS186
|
4.8
|
33.4
|
1.0
|
NE2
|
C:HIS76
|
5.0
|
30.5
|
1.0
|
CA
|
C:ASP20
|
5.0
|
29.7
|
1.0
|
|
Manganese binding site 6 out
of 6 in 1g5b
Go back to
Manganese Binding Sites List in 1g5b
Manganese binding site 6 out
of 6 in the Bacteriophage Lambda Ser/Thr Protein Phosphatase
Mono view
Stereo pair view
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A full contact list of Manganese with other atoms in the Mn binding
site number 6 of Bacteriophage Lambda Ser/Thr Protein Phosphatase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn1002
b:26.6
occ:1.00
|
OD1
|
C:ASN75
|
2.1
|
30.6
|
1.0
|
NE2
|
C:HIS139
|
2.2
|
27.7
|
1.0
|
OD2
|
C:ASP49
|
2.2
|
26.1
|
1.0
|
ND1
|
C:HIS186
|
2.3
|
28.2
|
1.0
|
O2
|
C:SO43003
|
2.3
|
31.4
|
1.0
|
O1
|
C:SO43003
|
2.4
|
33.9
|
1.0
|
S
|
C:SO43003
|
2.9
|
34.9
|
1.0
|
CE1
|
C:HIS139
|
3.0
|
25.2
|
1.0
|
CE1
|
C:HIS186
|
3.1
|
29.5
|
1.0
|
CG
|
C:ASP49
|
3.1
|
26.3
|
1.0
|
CG
|
C:ASN75
|
3.2
|
31.8
|
1.0
|
CD2
|
C:HIS139
|
3.3
|
28.9
|
1.0
|
CG
|
C:HIS186
|
3.4
|
30.5
|
1.0
|
OD1
|
C:ASP49
|
3.4
|
28.4
|
1.0
|
MN
|
C:MN1001
|
3.4
|
28.6
|
1.0
|
ND2
|
C:ASN75
|
3.6
|
26.2
|
1.0
|
O3
|
C:SO43003
|
3.8
|
31.6
|
1.0
|
CA
|
C:HIS186
|
3.8
|
29.7
|
1.0
|
CB
|
C:HIS186
|
3.9
|
29.6
|
1.0
|
OD2
|
C:ASP20
|
3.9
|
29.6
|
1.0
|
CD2
|
C:HIS76
|
4.0
|
26.2
|
1.0
|
O4
|
C:SO43003
|
4.1
|
25.8
|
1.0
|
ND1
|
C:HIS139
|
4.2
|
27.8
|
1.0
|
NE2
|
C:HIS186
|
4.3
|
28.4
|
1.0
|
CG
|
C:HIS139
|
4.4
|
29.8
|
1.0
|
CB
|
C:ASP49
|
4.4
|
24.7
|
1.0
|
O
|
C:HIS186
|
4.4
|
37.6
|
1.0
|
CD2
|
C:HIS186
|
4.5
|
28.2
|
1.0
|
CB
|
C:ASN75
|
4.5
|
29.1
|
1.0
|
O
|
C:ILE159
|
4.5
|
31.0
|
1.0
|
N
|
C:ASN75
|
4.6
|
28.2
|
1.0
|
C
|
C:HIS186
|
4.6
|
33.4
|
1.0
|
N
|
C:HIS186
|
4.7
|
31.3
|
1.0
|
NE2
|
C:HIS76
|
4.7
|
30.5
|
1.0
|
|
Reference:
W.C.Voegtli,
D.J.White,
N.J.Reiter,
F.Rusnak,
A.C.Rosenzweig.
Structure of the Bacteriophage Lambda Ser/Thr Protein Phosphatase with Sulfate Ion Bound in Two Coordination Modes. Biochemistry V. 39 15365 2000.
ISSN: ISSN 0006-2960
PubMed: 11112522
DOI: 10.1021/BI0021030
Page generated: Sat Oct 5 10:45:31 2024
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