Atomistry » Manganese » PDB 6a9v-6bh4 » 6ah7
Atomistry »
  Manganese »
    PDB 6a9v-6bh4 »
      6ah7 »

Manganese in PDB 6ah7: D45W/H226G Mutant of Marine Bacterial Prolidase

Enzymatic activity of D45W/H226G Mutant of Marine Bacterial Prolidase

All present enzymatic activity of D45W/H226G Mutant of Marine Bacterial Prolidase:
3.4.13.9;

Protein crystallography data

The structure of D45W/H226G Mutant of Marine Bacterial Prolidase, PDB code: 6ah7 was solved by Y.Jian, X.Yunzhu, L.Lijuan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 67.29 / 2.38
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 183.632, 183.632, 371.306, 90.00, 90.00, 120.00
R / Rfree (%) 23.3 / 26.9

Other elements in 6ah7:

The structure of D45W/H226G Mutant of Marine Bacterial Prolidase also contains other interesting chemical elements:

Sodium (Na) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the D45W/H226G Mutant of Marine Bacterial Prolidase (pdb code 6ah7). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 8 binding sites of Manganese where determined in the D45W/H226G Mutant of Marine Bacterial Prolidase, PDB code: 6ah7:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Manganese binding site 1 out of 8 in 6ah7

Go back to Manganese Binding Sites List in 6ah7
Manganese binding site 1 out of 8 in the D45W/H226G Mutant of Marine Bacterial Prolidase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of D45W/H226G Mutant of Marine Bacterial Prolidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn501

b:46.1
occ:1.00
OD2 A:ASP255 2.1 41.2 1.0
NE2 A:HIS336 2.3 37.5 1.0
OE2 A:GLU420 2.3 46.2 1.0
OE1 A:GLU381 2.8 44.3 1.0
CE1 A:HIS336 3.0 36.1 1.0
CG A:ASP255 3.1 40.7 1.0
CD A:GLU420 3.2 45.3 1.0
MN A:MN502 3.2 50.1 1.0
CD A:GLU381 3.3 41.7 1.0
CD2 A:HIS336 3.3 38.0 1.0
OE1 A:GLU420 3.4 44.6 1.0
OE2 A:GLU381 3.5 40.9 1.0
OD1 A:ASP255 3.7 38.2 1.0
OG1 A:THR379 3.8 34.3 1.0
CG2 A:THR379 3.8 32.5 1.0
CB A:THR379 4.0 35.8 1.0
ND1 A:HIS336 4.1 43.1 1.0
CB A:ASP255 4.3 38.2 1.0
CG A:HIS336 4.3 40.6 1.0
CG A:GLU381 4.5 40.5 1.0
CG A:GLU420 4.6 39.2 1.0
CE1 A:HIS343 4.6 41.8 0.4
NE2 A:HIS343 4.8 40.0 0.4
O A:ASP255 4.9 35.2 1.0

Manganese binding site 2 out of 8 in 6ah7

Go back to Manganese Binding Sites List in 6ah7
Manganese binding site 2 out of 8 in the D45W/H226G Mutant of Marine Bacterial Prolidase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of D45W/H226G Mutant of Marine Bacterial Prolidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn502

b:50.1
occ:1.00
OD1 A:ASP255 2.1 38.2 1.0
OE1 A:GLU420 2.3 44.6 1.0
OD1 A:ASP244 2.4 38.6 1.0
OD2 A:ASP244 2.4 39.8 1.0
CG A:ASP244 2.7 38.9 1.0
CG A:ASP255 2.9 40.7 1.0
OD2 A:ASP255 3.1 41.2 1.0
MN A:MN501 3.2 46.1 1.0
CD A:GLU420 3.2 45.3 1.0
OE2 A:GLU420 3.5 46.2 1.0
OG1 A:THR257 3.6 36.3 1.0
OH A:TYR212 3.8 32.4 1.0
OE2 A:GLU381 4.1 40.9 1.0
CZ A:TYR212 4.2 34.1 1.0
CB A:ASP244 4.2 35.9 1.0
CB A:ASP255 4.3 38.2 1.0
C A:ASP255 4.5 33.9 1.0
CE2 A:TYR212 4.5 38.5 1.0
O A:ASP255 4.5 35.2 1.0
CG A:GLU420 4.6 39.2 1.0
CA A:ASP255 4.7 32.8 1.0
NE A:ARG418 4.9 41.6 1.0
N A:ILE256 4.9 32.0 1.0
CD A:GLU381 4.9 41.7 1.0
CE1 A:TYR212 4.9 34.8 1.0
NH2 A:ARG418 5.0 36.1 1.0

Manganese binding site 3 out of 8 in 6ah7

Go back to Manganese Binding Sites List in 6ah7
Manganese binding site 3 out of 8 in the D45W/H226G Mutant of Marine Bacterial Prolidase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of D45W/H226G Mutant of Marine Bacterial Prolidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn501

b:50.5
occ:1.00
OE2 B:GLU420 2.1 38.5 1.0
OD2 B:ASP255 2.1 44.1 1.0
O B:HOH625 2.1 45.5 1.0
NE2 B:HIS336 2.3 37.3 1.0
OE2 B:GLU381 2.7 43.6 1.0
CE1 B:HIS336 3.0 38.8 1.0
CG B:ASP255 3.1 38.3 1.0
CD B:GLU420 3.2 37.8 1.0
MN B:MN502 3.3 48.6 1.0
CD B:GLU381 3.3 45.2 1.0
CD2 B:HIS336 3.4 37.7 1.0
OE1 B:GLU381 3.5 45.0 1.0
OD1 B:ASP255 3.6 37.9 1.0
OE1 B:GLU420 3.6 42.7 1.0
CG2 B:THR379 3.7 33.5 1.0
OG1 B:THR379 3.8 38.8 1.0
CB B:THR379 3.9 37.1 1.0
ND1 B:HIS336 4.1 40.9 1.0
CB B:ASP255 4.2 38.0 1.0
CG B:HIS336 4.4 39.2 1.0
CG B:GLU420 4.4 38.5 1.0
CG B:GLU381 4.5 39.3 1.0
NE2 B:HIS343 4.6 41.1 0.5
O B:HOH703 4.7 62.5 1.0
O B:ASP255 4.9 40.8 1.0

Manganese binding site 4 out of 8 in 6ah7

Go back to Manganese Binding Sites List in 6ah7
Manganese binding site 4 out of 8 in the D45W/H226G Mutant of Marine Bacterial Prolidase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of D45W/H226G Mutant of Marine Bacterial Prolidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn502

b:48.6
occ:1.00
OD1 B:ASP255 2.1 37.9 1.0
OD1 B:ASP244 2.3 39.2 1.0
O B:HOH625 2.3 45.5 1.0
OE1 B:GLU420 2.5 42.7 1.0
OD2 B:ASP244 2.6 40.5 1.0
CG B:ASP244 2.8 41.6 1.0
CG B:ASP255 2.9 38.3 1.0
O B:HOH703 3.1 62.5 1.0
OD2 B:ASP255 3.1 44.1 1.0
CD B:GLU420 3.3 37.8 1.0
MN B:MN501 3.3 50.5 1.0
OE2 B:GLU420 3.3 38.5 1.0
OG1 B:THR257 3.6 34.7 1.0
OH B:TYR212 3.7 37.9 1.0
OE1 B:GLU381 4.1 45.0 1.0
CZ B:TYR212 4.2 37.6 1.0
CB B:ASP244 4.3 39.8 1.0
CB B:ASP255 4.3 38.0 1.0
O B:HOH700 4.4 53.5 1.0
CE2 B:TYR212 4.4 40.5 1.0
C B:ASP255 4.5 37.7 1.0
O B:ASP255 4.7 40.8 1.0
CA B:ASP255 4.7 33.2 1.0
CG B:GLU420 4.7 38.5 1.0
N B:ILE256 4.7 33.8 1.0
CD B:GLU381 4.8 45.2 1.0
O B:ILE256 4.8 39.1 1.0
CE1 B:TYR212 4.9 33.6 1.0
NE B:ARG418 4.9 42.1 1.0
OE2 B:GLU381 4.9 43.6 1.0
C B:ILE256 5.0 39.3 1.0

Manganese binding site 5 out of 8 in 6ah7

Go back to Manganese Binding Sites List in 6ah7
Manganese binding site 5 out of 8 in the D45W/H226G Mutant of Marine Bacterial Prolidase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of D45W/H226G Mutant of Marine Bacterial Prolidase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn501

b:52.8
occ:1.00
NE2 C:HIS336 2.2 44.5 1.0
OE2 C:GLU420 2.2 41.4 1.0
OD2 C:ASP255 2.3 45.3 1.0
OE1 C:GLU381 2.7 52.8 1.0
CE1 C:HIS336 2.9 46.5 1.0
CD C:GLU381 2.9 50.6 1.0
OE2 C:GLU381 2.9 45.6 1.0
MN C:MN502 3.1 53.9 1.0
CD C:GLU420 3.2 47.5 1.0
CG C:ASP255 3.3 44.3 1.0
CD2 C:HIS336 3.3 45.3 1.0
OE1 C:GLU420 3.6 51.2 1.0
CG2 C:THR379 3.7 40.6 1.0
OD1 C:ASP255 3.8 43.8 1.0
CG C:GLU381 3.9 45.7 1.0
CB C:THR379 4.1 37.0 1.0
ND1 C:HIS336 4.1 49.6 1.0
OG1 C:THR379 4.1 44.4 1.0
CG C:HIS336 4.3 44.0 1.0
CE1 C:HIS343 4.5 46.9 0.4
CB C:ASP255 4.5 43.1 1.0
CG C:GLU420 4.5 47.8 1.0
O C:HOH692 4.9 46.8 1.0
O C:HOH660 4.9 59.3 1.0
CG1 C:VAL342 5.0 43.8 1.0

Manganese binding site 6 out of 8 in 6ah7

Go back to Manganese Binding Sites List in 6ah7
Manganese binding site 6 out of 8 in the D45W/H226G Mutant of Marine Bacterial Prolidase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of D45W/H226G Mutant of Marine Bacterial Prolidase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn502

b:53.9
occ:1.00
OE1 C:GLU420 2.2 51.2 1.0
OD1 C:ASP255 2.3 43.8 1.0
OD2 C:ASP244 2.3 50.4 1.0
OD1 C:ASP244 2.4 47.4 1.0
CG C:ASP244 2.7 45.9 1.0
CG C:ASP255 3.0 44.3 1.0
CD C:GLU420 3.0 47.5 1.0
OD2 C:ASP255 3.1 45.3 1.0
MN C:MN501 3.1 52.8 1.0
OE2 C:GLU420 3.2 41.4 1.0
OE1 C:GLU381 3.2 52.8 1.0
OG1 C:THR257 3.6 42.7 1.0
O C:HOH665 4.0 49.8 1.0
OH C:TYR212 4.1 38.6 1.0
CB C:ASP244 4.2 43.0 1.0
CD C:GLU381 4.3 50.6 1.0
O C:HOH692 4.4 46.8 1.0
CB C:ASP255 4.5 43.1 1.0
CG C:GLU420 4.5 47.8 1.0
CZ C:TYR212 4.5 37.8 1.0
NH2 C:ARG418 4.6 45.1 1.0
CE2 C:TYR212 4.7 42.5 1.0
C C:ASP255 4.7 43.9 1.0
O C:ASP255 4.8 48.5 1.0
NE C:ARG418 4.9 49.2 1.0
N C:ILE256 4.9 41.7 1.0
CB C:GLU420 4.9 47.6 1.0
CA C:ASP255 4.9 41.6 1.0
OE2 C:GLU381 5.0 45.6 1.0

Manganese binding site 7 out of 8 in 6ah7

Go back to Manganese Binding Sites List in 6ah7
Manganese binding site 7 out of 8 in the D45W/H226G Mutant of Marine Bacterial Prolidase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 7 of D45W/H226G Mutant of Marine Bacterial Prolidase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn501

b:44.1
occ:1.00
OE2 D:GLU420 1.5 44.3 1.0
OE2 D:GLU381 2.1 43.2 1.0
NE2 D:HIS336 2.1 37.4 1.0
OD2 D:ASP255 2.1 40.4 1.0
CD D:GLU381 2.3 46.2 1.0
OE1 D:GLU381 2.3 43.7 1.0
CD D:GLU420 2.8 39.2 1.0
O D:HOH601 2.8 58.7 1.0
CE1 D:HIS336 2.8 39.1 1.0
CG D:ASP255 3.1 40.2 1.0
MN D:MN502 3.2 50.4 1.0
CD2 D:HIS336 3.2 35.7 1.0
OE1 D:GLU420 3.4 42.4 1.0
CG D:GLU381 3.6 36.9 1.0
OD1 D:ASP255 3.6 35.9 1.0
OG1 D:THR379 3.7 30.8 1.0
CG2 D:THR379 3.9 36.4 1.0
ND1 D:HIS336 4.0 39.9 1.0
CG D:GLU420 4.0 40.1 1.0
CB D:THR379 4.1 35.9 1.0
CG D:HIS336 4.2 37.9 1.0
CB D:ASP255 4.3 37.1 1.0
CE1 D:HIS343 4.5 38.1 0.5
O D:HOH646 4.8 49.3 1.0
NE2 D:HIS343 4.8 39.0 0.5
CG1 D:VAL342 4.9 43.6 1.0
CB D:GLU381 4.9 38.9 1.0

Manganese binding site 8 out of 8 in 6ah7

Go back to Manganese Binding Sites List in 6ah7
Manganese binding site 8 out of 8 in the D45W/H226G Mutant of Marine Bacterial Prolidase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 8 of D45W/H226G Mutant of Marine Bacterial Prolidase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn502

b:50.4
occ:1.00
OE1 D:GLU420 1.8 42.4 1.0
OD1 D:ASP255 2.1 35.9 1.0
O D:HOH601 2.3 58.7 1.0
OD2 D:ASP244 2.4 41.1 1.0
OD1 D:ASP244 2.6 40.1 1.0
CD D:GLU420 2.7 39.2 1.0
CG D:ASP244 2.8 39.7 1.0
CG D:ASP255 2.9 40.2 1.0
OE2 D:GLU420 2.9 44.3 1.0
OD2 D:ASP255 3.0 40.4 1.0
MN D:MN501 3.2 44.1 1.0
OE1 D:GLU381 3.4 43.7 1.0
OG1 D:THR257 3.5 37.1 1.0
CD D:GLU381 3.9 46.2 1.0
OH D:TYR212 4.0 39.8 1.0
CG D:GLU420 4.1 40.1 1.0
CB D:ASP255 4.3 37.1 1.0
CG D:GLU381 4.3 36.9 1.0
CB D:ASP244 4.3 35.5 1.0
CZ D:TYR212 4.4 39.3 1.0
O D:ASP255 4.5 37.5 1.0
C D:ASP255 4.5 39.4 1.0
CE2 D:TYR212 4.6 40.4 1.0
CB D:GLU420 4.7 39.7 1.0
OE2 D:GLU381 4.7 43.2 1.0
CA D:ASP255 4.7 34.8 1.0
NE D:ARG418 4.8 43.2 1.0
N D:ILE256 4.9 36.9 1.0
CB D:THR257 5.0 40.3 1.0

Reference:

Y.Jian, X.Yunzhu. D45W/H226G Mutant of Marine Bacterial Prolidase To Be Published.
Page generated: Tue Dec 15 04:50:31 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy