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Manganese in PDB 3m7v: Crystal Structure of Phosphopentomutase From Streptococcus Mutans

Enzymatic activity of Crystal Structure of Phosphopentomutase From Streptococcus Mutans

All present enzymatic activity of Crystal Structure of Phosphopentomutase From Streptococcus Mutans:
5.4.2.7;

Protein crystallography data

The structure of Crystal Structure of Phosphopentomutase From Streptococcus Mutans, PDB code: 3m7v was solved by A.A.Fedorov, J.Bonanno, E.V.Fedorov, S.K.Burley, S.C.Almo, New York Sgxresearch Center For Structural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 69.788, 63.687, 104.765, 90.00, 98.85, 90.00
R / Rfree (%) 18.1 / 21.1

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Phosphopentomutase From Streptococcus Mutans (pdb code 3m7v). 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 Phosphopentomutase From Streptococcus Mutans, PDB code: 3m7v:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 3m7v

Go back to Manganese Binding Sites List in 3m7v
Manganese binding site 1 out of 4 in the Crystal Structure of Phosphopentomutase From Streptococcus Mutans


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 Phosphopentomutase From Streptococcus Mutans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn412

b:30.5
occ:1.00
OD2 A:ASP13 1.9 30.0 1.0
OD2 A:ASP339 2.0 28.3 1.0
NE2 A:HIS340 2.1 27.6 1.0
CG A:ASP13 2.6 32.7 1.0
OD1 A:ASP13 2.6 32.4 1.0
CG A:ASP339 2.8 28.2 1.0
OD1 A:ASP339 2.9 29.7 1.0
CD2 A:HIS340 3.0 27.3 1.0
CE1 A:HIS340 3.2 27.5 1.0
CB A:THR92 3.7 37.0 1.0
OG1 A:THR92 3.9 41.3 1.0
CA A:THR92 3.9 35.2 1.0
CB A:ASP13 4.0 31.1 1.0
CG A:HIS340 4.1 27.2 1.0
CE1 A:HIS351 4.1 32.1 1.0
ND1 A:HIS340 4.2 27.5 1.0
CB A:ASP339 4.2 27.5 1.0
N A:SER14 4.3 29.6 1.0
CG A:ASP298 4.4 32.0 1.0
OD1 A:ASP298 4.5 33.6 1.0
CA A:ASP13 4.5 30.6 1.0
NE2 A:HIS351 4.5 30.9 1.0
N A:THR92 4.5 33.5 1.0
OD2 A:ASP298 4.6 29.0 1.0
CE1 A:HIS96 4.6 30.6 1.0
C A:ASP13 4.6 29.9 1.0
ND1 A:HIS351 4.8 31.6 1.0
CB A:ASP298 4.9 32.9 1.0
MN A:MN413 4.9 34.0 1.0
CA A:SER14 5.0 29.2 1.0

Manganese binding site 2 out of 4 in 3m7v

Go back to Manganese Binding Sites List in 3m7v
Manganese binding site 2 out of 4 in the Crystal Structure of Phosphopentomutase From Streptococcus Mutans


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 Phosphopentomutase From Streptococcus Mutans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn413

b:34.0
occ:1.00
OD1 A:ASP298 2.0 33.6 1.0
NE2 A:HIS351 2.0 30.9 1.0
NE2 A:HIS303 2.2 35.9 1.0
CG A:ASP298 2.8 32.0 1.0
OD2 A:ASP298 2.9 29.0 1.0
CE1 A:HIS351 3.0 32.1 1.0
CD2 A:HIS351 3.0 29.6 1.0
CD2 A:HIS303 3.1 36.0 1.0
CE1 A:HIS303 3.2 34.6 1.0
ND1 A:HIS351 4.1 31.6 1.0
CG A:HIS351 4.1 28.7 1.0
CB A:ASP298 4.2 32.9 1.0
CG A:HIS303 4.2 35.7 1.0
ND1 A:HIS303 4.3 36.5 1.0
OD2 A:ASP165 4.3 62.6 1.0
ND2 A:ASN342 4.5 28.2 1.0
O A:HOH459 4.5 29.5 1.0
CE1 A:HIS340 4.6 27.5 1.0
NE2 A:HIS340 4.8 27.6 1.0
CB A:ALA164 4.8 53.6 1.0
MN A:MN412 4.9 30.5 1.0

Manganese binding site 3 out of 4 in 3m7v

Go back to Manganese Binding Sites List in 3m7v
Manganese binding site 3 out of 4 in the Crystal Structure of Phosphopentomutase From Streptococcus Mutans


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 Phosphopentomutase From Streptococcus Mutans within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn412

b:27.5
occ:1.00
OD2 B:ASP339 2.0 28.4 1.0
OD2 B:ASP13 2.0 29.0 1.0
NE2 B:HIS340 2.1 23.7 1.0
CG B:ASP13 2.6 28.2 1.0
OD1 B:ASP13 2.7 30.2 1.0
CG B:ASP339 2.8 25.6 1.0
CD2 B:HIS340 2.9 25.7 1.0
OD1 B:ASP339 2.9 26.7 1.0
CE1 B:HIS340 3.2 25.3 1.0
CB B:THR92 3.7 31.7 1.0
CA B:THR92 3.9 29.5 1.0
OG1 B:THR92 4.0 35.0 1.0
CG B:HIS340 4.1 26.7 1.0
CB B:ASP13 4.1 27.2 1.0
ND1 B:HIS340 4.2 26.9 1.0
CE1 B:HIS351 4.2 31.0 1.0
CB B:ASP339 4.2 23.8 1.0
OD1 B:ASP298 4.4 31.0 1.0
N B:SER14 4.4 26.3 1.0
CG B:ASP298 4.4 30.8 1.0
NE2 B:HIS351 4.5 30.1 1.0
CA B:ASP13 4.5 26.3 1.0
N B:THR92 4.6 29.1 1.0
CE1 B:HIS96 4.6 26.0 1.0
OD2 B:ASP298 4.6 29.3 1.0
C B:ASP13 4.7 26.8 1.0
ND1 B:HIS351 4.8 30.3 1.0
CB B:ASP298 4.9 29.0 1.0
CA B:SER14 5.0 26.5 1.0
MN B:MN413 5.0 34.4 1.0

Manganese binding site 4 out of 4 in 3m7v

Go back to Manganese Binding Sites List in 3m7v
Manganese binding site 4 out of 4 in the Crystal Structure of Phosphopentomutase From Streptococcus Mutans


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 Phosphopentomutase From Streptococcus Mutans within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn413

b:34.4
occ:1.00
OD1 B:ASP298 2.0 31.0 1.0
NE2 B:HIS303 2.0 34.9 1.0
NE2 B:HIS351 2.1 30.1 1.0
CG B:ASP298 2.8 30.8 1.0
OD2 B:ASP298 3.0 29.3 1.0
CD2 B:HIS303 3.0 38.4 1.0
CD2 B:HIS351 3.0 30.2 1.0
CE1 B:HIS303 3.1 39.7 1.0
CE1 B:HIS351 3.1 31.0 1.0
O B:HOH504 3.7 37.8 1.0
ND1 B:HIS303 4.2 38.1 1.0
CG B:HIS303 4.2 36.7 1.0
CG B:HIS351 4.2 29.8 1.0
ND1 B:HIS351 4.2 30.3 1.0
OD1 B:ASP165 4.2 50.8 1.0
CB B:ASP298 4.2 29.0 1.0
ND2 B:ASN342 4.5 29.4 1.0
CE1 B:HIS340 4.7 25.3 1.0
O B:HOH425 4.8 29.8 1.0
NE2 B:HIS340 4.8 23.7 1.0
MN B:MN412 5.0 27.5 1.0

Reference:

A.A.Fedorov, J.Bonanno, E.V.Fedorov, S.K.Burley, S.C.Almo. Crystal Structure of Phosphopentomutase From Streptococcus Mutans To Be Published.
Page generated: Tue Dec 15 04:12:16 2020

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