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Manganese in PDB 7n02: X-Ray Crystallographic Structure Model of Lactococcus Lactis Prolidase Mutant D36S

Enzymatic activity of X-Ray Crystallographic Structure Model of Lactococcus Lactis Prolidase Mutant D36S

All present enzymatic activity of X-Ray Crystallographic Structure Model of Lactococcus Lactis Prolidase Mutant D36S:
3.4.13.9;

Protein crystallography data

The structure of X-Ray Crystallographic Structure Model of Lactococcus Lactis Prolidase Mutant D36S, PDB code: 7n02 was solved by S.Xu, P.Grochulski, T.Tanaka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.64 / 2.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 83.12, 87.27, 119.4, 90, 90, 90
R / Rfree (%) 21.2 / 27

Manganese Binding Sites:

The binding sites of Manganese atom in the X-Ray Crystallographic Structure Model of Lactococcus Lactis Prolidase Mutant D36S (pdb code 7n02). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the X-Ray Crystallographic Structure Model of Lactococcus Lactis Prolidase Mutant D36S, PDB code: 7n02:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 7n02

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Manganese binding site 1 out of 4 in the X-Ray Crystallographic Structure Model of Lactococcus Lactis Prolidase Mutant D36S


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of X-Ray Crystallographic Structure Model of Lactococcus Lactis Prolidase Mutant D36S within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:51.5
occ:1.00
OD1 A:ASP232 2.2 48.3 1.0
O A:HOH521 2.2 53.5 1.0
OD1 A:ASP221 2.2 44.3 1.0
OE1 A:GLU339 2.4 48.4 1.0
O A:HOH580 2.5 47.3 1.0
OD2 A:ASP221 2.5 43.4 1.0
CG A:ASP221 2.7 45.8 1.0
CG A:ASP232 3.1 43.7 1.0
CD A:GLU339 3.1 46.7 1.0
OE2 A:GLU339 3.2 43.6 1.0
OD2 A:ASP232 3.2 43.8 1.0
MN A:MN402 3.4 52.6 1.0
OG1 A:THR234 3.8 39.8 1.0
CZ A:PHE190 3.9 50.3 1.0
O A:HOH581 4.0 53.6 1.0
O A:HOH583 4.0 52.8 1.0
CB A:ASP221 4.3 44.5 1.0
CE2 A:PHE190 4.4 50.4 1.0
OE1 A:GLU325 4.4 53.2 1.0
N A:ALA233 4.4 45.4 1.0
CB A:ASP232 4.5 43.2 1.0
CE1 A:PHE190 4.5 55.7 1.0
O A:ALA233 4.6 46.6 1.0
CG A:GLU339 4.6 46.5 1.0
C A:ALA233 4.7 45.1 1.0
C A:ASP232 4.9 45.8 1.0
CA A:ASP232 5.0 44.0 1.0
NE A:ARG337 5.0 47.3 1.0

Manganese binding site 2 out of 4 in 7n02

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Manganese binding site 2 out of 4 in the X-Ray Crystallographic Structure Model of Lactococcus Lactis Prolidase Mutant D36S


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of X-Ray Crystallographic Structure Model of Lactococcus Lactis Prolidase Mutant D36S within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn402

b:52.6
occ:1.00
O A:HOH521 2.2 53.5 1.0
OE2 A:GLU339 2.3 43.6 1.0
OD2 A:ASP232 2.3 43.8 1.0
NE2 A:HIS296 2.4 50.6 1.0
OE2 A:GLU325 2.5 51.2 1.0
O A:HOH581 2.5 53.6 1.0
CG A:ASP232 3.2 43.7 1.0
CD A:GLU325 3.3 47.6 1.0
CD2 A:HIS296 3.3 52.8 1.0
CE1 A:HIS296 3.4 47.8 1.0
MN A:MN401 3.4 51.5 1.0
CD A:GLU339 3.4 46.7 1.0
OE1 A:GLU325 3.5 53.2 1.0
OD1 A:ASP232 3.7 48.3 1.0
O A:HOH580 3.8 47.3 1.0
OE1 A:GLU339 3.9 48.4 1.0
OG A:SER323 4.2 46.7 1.0
CB A:SER323 4.3 50.0 1.0
CB A:ASP232 4.4 43.2 1.0
ND1 A:HIS296 4.5 54.2 1.0
CG A:HIS296 4.5 55.3 1.0
CG A:GLU339 4.6 46.5 1.0
CG A:GLU325 4.7 44.6 1.0
NE2 A:HIS303 5.0 65.7 1.0

Manganese binding site 3 out of 4 in 7n02

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Manganese binding site 3 out of 4 in the X-Ray Crystallographic Structure Model of Lactococcus Lactis Prolidase Mutant D36S


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of X-Ray Crystallographic Structure Model of Lactococcus Lactis Prolidase Mutant D36S within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn401

b:50.6
occ:1.00
O B:HOH540 2.2 51.7 1.0
OD1 B:ASP232 2.2 53.5 1.0
OD1 B:ASP221 2.3 49.1 1.0
O B:HOH557 2.3 62.1 1.0
OE1 B:GLU339 2.3 50.9 1.0
OD2 B:ASP221 2.7 43.1 1.0
CG B:ASP221 2.9 47.6 1.0
CG B:ASP232 3.1 51.8 1.0
CD B:GLU339 3.1 52.8 1.0
OE2 B:GLU339 3.2 47.9 1.0
OD2 B:ASP232 3.3 51.5 1.0
MN B:MN402 3.5 54.3 1.0
OG1 B:THR234 3.9 46.4 1.0
CZ B:PHE190 3.9 52.2 1.0
O B:HOH580 3.9 54.9 1.0
O B:ALA233 4.2 45.0 1.0
CB B:ASP221 4.4 47.5 1.0
OE1 B:GLU325 4.4 54.2 1.0
N B:ALA233 4.4 48.9 1.0
CE1 B:PHE190 4.5 52.7 1.0
CE2 B:PHE190 4.5 52.1 1.0
CB B:ASP232 4.5 48.0 1.0
CG B:GLU339 4.6 48.1 1.0
C B:ALA233 4.6 48.5 1.0
C B:ASP232 4.8 48.6 1.0
CA B:ALA233 4.9 51.9 1.0
CA B:ASP232 5.0 48.6 1.0

Manganese binding site 4 out of 4 in 7n02

Go back to Manganese Binding Sites List in 7n02
Manganese binding site 4 out of 4 in the X-Ray Crystallographic Structure Model of Lactococcus Lactis Prolidase Mutant D36S


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of X-Ray Crystallographic Structure Model of Lactococcus Lactis Prolidase Mutant D36S within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn402

b:54.3
occ:1.00
NE2 B:HIS296 2.3 53.4 1.0
O B:HOH580 2.3 54.9 1.0
OE2 B:GLU339 2.3 47.9 1.0
OE2 B:GLU325 2.3 53.4 1.0
OD2 B:ASP232 2.4 51.5 1.0
O B:HOH540 2.5 51.7 1.0
CD B:GLU325 3.2 58.0 1.0
CE1 B:HIS296 3.2 49.5 1.0
CD2 B:HIS296 3.2 52.0 1.0
OE1 B:GLU325 3.3 54.2 1.0
CG B:ASP232 3.4 51.8 1.0
CD B:GLU339 3.4 52.8 1.0
MN B:MN401 3.5 50.6 1.0
O B:HOH557 3.7 62.1 1.0
OD1 B:ASP232 3.8 53.5 1.0
OE1 B:GLU339 3.9 50.9 1.0
OG B:SER323 4.3 49.7 1.0
ND1 B:HIS296 4.4 51.1 1.0
CG B:HIS296 4.4 54.4 1.0
CB B:SER323 4.5 50.0 1.0
CB B:ASP232 4.6 48.0 1.0
CG B:GLU325 4.6 47.4 1.0
CG B:GLU339 4.7 48.1 1.0

Reference:

O.Kgosisejo, J.A.Chen, P.Grochulski, T.Tanaka. Crystallographic Structure of Recombinant Lactococcus Lactis Prolidase to Support Proposed Structure-Function Relationships. Biochim Biophys Acta V.1865 473 2017PROTEINS Proteom.
ISSN: ISSN 1570-9639
PubMed: 28179139
DOI: 10.1016/J.BBAPAP.2017.02.004
Page generated: Sun Oct 6 10:13:10 2024

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