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Osmium in PDB 1rmq: Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate

Enzymatic activity of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate

All present enzymatic activity of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate:
3.1.3.2;

Protein crystallography data

The structure of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate, PDB code: 1rmq was solved by V.Calderone, C.Forleo, M.Benvenuti, G.M.Rossolini, M.C.Thaller, S.Mangani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.732, 66.447, 91.523, 90.00, 121.30, 90.00
R / Rfree (%) 18.3 / 23

Other elements in 1rmq:

The structure of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate also contains other interesting chemical elements:

Cobalt (Co) 2 atoms

Osmium Binding Sites:

The binding sites of Osmium atom in the Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate (pdb code 1rmq). This binding sites where shown within 5.0 Angstroms radius around Osmium atom.
In total 4 binding sites of Osmium where determined in the Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate, PDB code: 1rmq:
Jump to Osmium binding site number: 1; 2; 3; 4;

Osmium binding site 1 out of 4 in 1rmq

Go back to Osmium Binding Sites List in 1rmq
Osmium binding site 1 out of 4 in the Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate


Mono view


Stereo pair view

A full contact list of Osmium with other atoms in the Os binding site number 1 of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Os402

b:84.0
occ:1.00
 OD1 A:ASP44 2.5 15.9 1.0
O A:HOH442 2.6 21.8 1.0
CO A:CO401 3.2 17.7 1.0
O A:HOH408 3.3 16.6 1.0
CG A:ASP44 3.4 19.6 1.0
OD2 A:ASP44 3.5 15.4 1.0
NZ A:LYS152 3.9 38.8 1.0
O A:HOH512 4.0 62.5 1.0
O A:HOH547 4.1 36.6 1.0
N A:GLY113 4.2 24.3 1.0
OD2 A:ASP46 4.2 16.6 1.0
N A:ASP46 4.2 18.0 1.0
O A:HOH428 4.3 15.8 1.0
CB A:ASP46 4.3 17.6 1.0
OG1 A:THR112 4.4 22.1 1.0
O A:ASP46 4.6 16.5 1.0
N A:ILE45 4.6 17.6 1.0
CG A:ASP46 4.7 19.7 1.0
CB A:ASP44 4.7 17.5 1.0
CA A:ASP46 4.8 17.5 1.0
CA A:THR112 4.8 21.1 1.0
CA A:GLY113 4.9 23.3 1.0
CE A:LYS152 5.0 40.5 1.0

Osmium binding site 2 out of 4 in 1rmq

Go back to Osmium Binding Sites List in 1rmq
Osmium binding site 2 out of 4 in the Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate


Mono view


Stereo pair view

A full contact list of Osmium with other atoms in the Os binding site number 2 of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Os405

b:40.0
occ:0.40
 NE2 A:HIS22 2.2 42.4 1.0
CD2 A:HIS22 3.2 35.2 1.0
CE1 A:HIS22 3.3 43.3 1.0
CG1 A:VAL24 4.1 23.3 1.0
ND1 A:HIS22 4.3 43.5 1.0
CG A:HIS22 4.4 34.8 1.0
OE2 A:GLU205 4.8 25.6 1.0
CG A:GLU205 5.0 21.1 1.0

Osmium binding site 3 out of 4 in 1rmq

Go back to Osmium Binding Sites List in 1rmq
Osmium binding site 3 out of 4 in the Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate


Mono view


Stereo pair view

A full contact list of Osmium with other atoms in the Os binding site number 3 of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Os404

b:95.4
occ:1.00
 OD1 B:ASP44 2.3 16.9 1.0
O B:HOH549 2.4 23.6 1.0
O B:HOH442 2.5 20.6 1.0
O B:HOH548 3.0 31.1 1.0
CG B:ASP44 3.3 21.9 1.0
CO B:CO403 3.4 19.2 1.0
OD2 B:ASP44 3.5 18.2 1.0
O B:HOH495 3.5 22.9 1.0
O B:HOH508 3.7 29.8 1.0
N B:ASP46 4.1 16.8 1.0
OD2 B:ASP46 4.3 24.3 1.0
N B:GLY113 4.3 23.6 1.0
OG1 B:THR112 4.3 23.4 1.0
CB B:ASP46 4.3 16.1 1.0
N B:ILE45 4.4 19.1 1.0
O B:HOH551 4.6 13.9 1.0
CB B:ASP44 4.6 20.4 1.0
CA B:ASP46 4.7 16.7 1.0
O B:ASP46 4.7 14.5 1.0
CG B:ASP46 4.7 21.9 1.0
CA B:THR112 4.8 23.7 1.0
CA B:GLY113 5.0 23.4 1.0

Osmium binding site 4 out of 4 in 1rmq

Go back to Osmium Binding Sites List in 1rmq
Osmium binding site 4 out of 4 in the Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate


Mono view


Stereo pair view

A full contact list of Osmium with other atoms in the Os binding site number 4 of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Os406

b:45.7
occ:0.40
 CE1 B:HIS22 2.2 39.4 1.0
NE2 B:HIS22 2.5 38.2 1.0
ND1 B:HIS22 3.5 39.0 1.0
CD2 B:HIS22 3.9 38.1 1.0
CG B:HIS22 4.3 34.3 1.0
OE2 B:GLU205 4.3 22.6 1.0
CG1 B:VAL24 4.4 19.0 1.0
ND1 A:HIS22 4.7 43.5 1.0
CG B:GLU205 4.9 19.0 1.0
CD B:GLU205 4.9 22.1 1.0
CE1 A:HIS22 5.0 43.3 1.0

Reference:

V.Calderone, C.Forleo, M.Benvenuti, G.M.Rossolini, M.C.Thaller, S.Mangani. Insights in the Catalytic Mechanism of Apha From Escherichia Coli To Be Published.
Page generated: Wed Dec 16 02:01:16 2020

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