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Manganese in PDB 3g1p: Crystals Structure of Phnp From E.Coli K-12

Protein crystallography data

The structure of Crystals Structure of Phnp From E.Coli K-12, PDB code: 3g1p was solved by K.Podzelinska, Z.Jia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 67.00 / 1.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 111.650, 75.405, 83.228, 90.00, 126.33, 90.00
R / Rfree (%) 18.6 / 21

Other elements in 3g1p:

The structure of Crystals Structure of Phnp From E.Coli K-12 also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystals Structure of Phnp From E.Coli K-12 (pdb code 3g1p). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystals Structure of Phnp From E.Coli K-12, PDB code: 3g1p:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 3g1p

Go back to Manganese Binding Sites List in 3g1p
Manganese binding site 1 out of 4 in the Crystals Structure of Phnp From E.Coli K-12


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystals Structure of Phnp From E.Coli K-12 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn400

b:11.3
occ:1.00
NE2 A:HIS143 2.2 12.9 1.0
O3 A:MLT500 2.2 18.0 1.0
ND1 A:HIS78 2.2 11.9 1.0
NE2 A:HIS76 2.2 9.3 1.0
OD2 A:ASP164 2.3 14.0 1.0
O1 A:MLT500 2.3 15.1 1.0
CE1 A:HIS143 3.1 13.0 1.0
C1 A:MLT500 3.1 19.2 1.0
CE1 A:HIS78 3.1 14.6 1.0
CD2 A:HIS76 3.1 9.1 1.0
C2 A:MLT500 3.2 20.4 1.0
CD2 A:HIS143 3.2 11.5 1.0
CE1 A:HIS76 3.2 8.8 1.0
CG A:HIS78 3.3 11.5 1.0
CG A:ASP164 3.3 15.7 1.0
CB A:HIS78 3.6 10.5 1.0
MN A:MN401 3.7 42.9 1.0
CB A:ASP164 3.8 16.3 1.0
C3 A:MLT500 4.0 21.6 1.0
ND1 A:HIS143 4.2 13.8 1.0
O A:HOH573 4.2 45.4 1.0
NE2 A:HIS78 4.3 15.6 1.0
O2 A:MLT500 4.3 20.4 1.0
CG A:HIS76 4.3 7.6 1.0
CG A:HIS143 4.3 12.9 1.0
ND1 A:HIS76 4.3 8.9 1.0
NE2 A:HIS81 4.4 12.6 1.0
CD2 A:HIS78 4.4 13.6 1.0
OD1 A:ASP164 4.4 17.1 1.0
CD2 A:HIS81 4.4 10.2 1.0
OD1 A:ASP80 4.5 18.5 1.0
CE1 A:HIS200 4.6 14.9 1.0
O A:HOH611 4.7 39.2 1.0
NE2 A:HIS200 4.9 15.5 1.0

Manganese binding site 2 out of 4 in 3g1p

Go back to Manganese Binding Sites List in 3g1p
Manganese binding site 2 out of 4 in the Crystals Structure of Phnp From E.Coli K-12


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystals Structure of Phnp From E.Coli K-12 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:42.9
occ:1.00
O A:HOH573 1.8 45.4 1.0
OD2 A:ASP164 2.1 14.0 1.0
NE2 A:HIS81 2.3 12.6 1.0
NE2 A:HIS222 2.6 16.8 1.0
OD1 A:ASP164 2.7 17.1 1.0
CG A:ASP164 2.7 15.7 1.0
O A:HOH320 3.1 24.1 1.0
OD2 A:ASP80 3.1 17.8 1.0
O3 A:MLT500 3.1 18.0 1.0
CD2 A:HIS81 3.2 10.2 1.0
CD2 A:HIS222 3.3 15.1 1.0
CE1 A:HIS81 3.3 11.8 1.0
MN A:MN400 3.7 11.3 1.0
CE1 A:HIS222 3.7 16.5 1.0
CG A:ASP80 3.8 14.9 1.0
OD1 A:ASP80 3.8 18.5 1.0
C2 A:MLT500 3.8 20.4 1.0
C1 A:MLT500 3.9 19.2 1.0
O1 A:MLT500 3.9 15.1 1.0
CE1 A:HIS200 4.1 14.9 1.0
CB A:ASP164 4.2 16.3 1.0
O A:HOH391 4.3 22.2 1.0
CG A:HIS81 4.4 9.5 1.0
CE1 A:HIS76 4.4 8.8 1.0
O A:HOH509 4.4 23.3 1.0
ND1 A:HIS81 4.4 11.1 1.0
NE2 A:HIS76 4.4 9.3 1.0
O2 A:MLT500 4.5 20.4 1.0
CG A:HIS222 4.5 12.2 1.0
ND1 A:HIS222 4.7 15.7 1.0
NE2 A:HIS200 4.8 15.5 1.0
O A:HOH657 4.9 95.9 1.0

Manganese binding site 3 out of 4 in 3g1p

Go back to Manganese Binding Sites List in 3g1p
Manganese binding site 3 out of 4 in the Crystals Structure of Phnp From E.Coli K-12


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystals Structure of Phnp From E.Coli K-12 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn402

b:9.3
occ:1.00
NE2 B:HIS143 2.2 10.2 1.0
NE2 B:HIS76 2.2 8.5 1.0
ND1 B:HIS78 2.2 11.9 1.0
O1 B:MLT501 2.2 13.6 1.0
OD2 B:ASP164 2.3 11.3 1.0
O3 B:MLT501 2.3 16.4 1.0
CE1 B:HIS78 3.1 10.7 1.0
CE1 B:HIS143 3.1 10.2 1.0
C1 B:MLT501 3.1 16.2 1.0
CD2 B:HIS76 3.1 8.8 1.0
CD2 B:HIS143 3.2 9.6 1.0
CE1 B:HIS76 3.2 8.6 1.0
C2 B:MLT501 3.3 17.4 1.0
CG B:HIS78 3.3 10.8 1.0
CG B:ASP164 3.3 12.3 1.0
MN B:MN403 3.5 26.4 1.0
CB B:HIS78 3.7 10.7 1.0
CB B:ASP164 3.8 13.9 1.0
O B:HOH623 4.0 30.4 1.0
C3 B:MLT501 4.1 20.5 1.0
ND1 B:HIS143 4.2 10.4 1.0
NE2 B:HIS78 4.2 12.7 1.0
O2 B:MLT501 4.3 18.8 1.0
CG B:HIS76 4.3 7.8 1.0
CG B:HIS143 4.3 11.1 1.0
ND1 B:HIS76 4.3 8.3 1.0
OD1 B:ASP164 4.3 14.7 1.0
NE2 B:HIS81 4.4 11.4 1.0
CD2 B:HIS78 4.4 13.2 1.0
O B:HOH394 4.4 73.2 1.0
CD2 B:HIS81 4.4 10.7 1.0
OD1 B:ASP80 4.6 16.7 1.0
CE1 B:HIS200 4.6 12.4 1.0
O B:HOH613 4.6 35.0 1.0
NE2 B:HIS200 4.9 12.7 1.0

Manganese binding site 4 out of 4 in 3g1p

Go back to Manganese Binding Sites List in 3g1p
Manganese binding site 4 out of 4 in the Crystals Structure of Phnp From E.Coli K-12


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystals Structure of Phnp From E.Coli K-12 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn403

b:26.4
occ:1.00
O B:HOH623 1.6 30.4 1.0
OD2 B:ASP164 2.0 11.3 1.0
NE2 B:HIS81 2.2 11.4 1.0
NE2 B:HIS222 2.5 15.5 1.0
CG B:ASP164 2.6 12.3 1.0
OD1 B:ASP164 2.7 14.7 1.0
OD2 B:ASP80 3.1 17.5 1.0
O3 B:MLT501 3.1 16.4 1.0
CD2 B:HIS81 3.1 10.7 1.0
CD2 B:HIS222 3.3 13.1 1.0
CE1 B:HIS81 3.3 11.0 1.0
MN B:MN402 3.5 9.3 1.0
CE1 B:HIS222 3.6 14.8 1.0
O B:HOH451 3.7 24.4 1.0
CG B:ASP80 3.8 13.4 1.0
C2 B:MLT501 3.8 17.4 1.0
O1 B:MLT501 3.8 13.6 1.0
OD1 B:ASP80 3.8 16.7 1.0
C1 B:MLT501 3.9 16.2 1.0
CB B:ASP164 4.1 13.9 1.0
CE1 B:HIS200 4.1 12.4 1.0
CE1 B:HIS76 4.2 8.6 1.0
NE2 B:HIS76 4.3 8.5 1.0
O B:HOH356 4.3 18.4 1.0
CG B:HIS81 4.3 10.0 1.0
ND1 B:HIS81 4.4 10.0 1.0
CG B:HIS222 4.5 11.9 1.0
O2 B:MLT501 4.5 18.8 1.0
ND1 B:HIS222 4.6 13.9 1.0
NE2 B:HIS200 4.8 12.7 1.0

Reference:

K.Podzelinska, S.He, M.Wathier, A.Yakunin, M.Proudftoot, B.Hove-Jensen, D.Zechel, Z.Jia. Crystals Structure of Phnp From E.Coli K-12 To Be Published.
Page generated: Sat Oct 5 16:22:40 2024

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