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Cobalt 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:

Osmium (Os) 4 atoms

Cobalt Binding Sites:

The binding sites of Cobalt 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 Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase with Osmiate Mimicking the Catalytic Intermediate, PDB code: 1rmq:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 1rmq

Go back to Cobalt Binding Sites List in 1rmq
Cobalt binding site 1 out of 2 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 Cobalt with other atoms in the Co 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:Co401

b:17.7
occ:1.00
OD2 A:ASP44 2.1 15.4 1.0
O A:HOH408 2.1 16.6 1.0
OD1 A:ASP167 2.1 16.5 1.0
O A:ASP46 2.2 16.5 1.0
O A:HOH428 2.2 15.8 1.0
CG A:ASP44 3.1 19.6 1.0
CG A:ASP167 3.1 16.1 1.0
OS A:OS402 3.2 84.0 1.0
C A:ASP46 3.3 18.4 1.0
OD2 A:ASP167 3.4 15.3 1.0
OD1 A:ASP44 3.5 15.9 1.0
OG A:SER168 3.9 19.5 1.0
OG1 A:THR48 3.9 18.2 1.0
N A:ASP46 3.9 18.0 1.0
CA A:ASP46 4.0 17.5 1.0
OD2 A:ASP171 4.0 18.4 1.0
O A:HOH420 4.1 19.6 1.0
CB A:ASP46 4.1 17.6 1.0
CB A:ASP44 4.4 17.5 1.0
CB A:ASP167 4.4 19.1 1.0
N A:ASP47 4.4 17.9 1.0
N A:ASP167 4.5 18.5 1.0
CB A:ASP47 4.6 16.2 1.0
O A:HOH442 4.6 21.8 1.0
N A:SER168 4.7 20.8 1.0
N A:THR48 4.7 16.1 1.0
C A:ILE45 4.8 17.8 1.0
CA A:ASP47 4.8 16.8 1.0
C A:ASP47 4.8 16.4 1.0
CB A:SER168 4.9 19.7 1.0
CB A:THR48 4.9 17.5 1.0
CA A:ASP167 5.0 18.5 1.0

Cobalt binding site 2 out of 2 in 1rmq

Go back to Cobalt Binding Sites List in 1rmq
Cobalt binding site 2 out of 2 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 Cobalt with other atoms in the Co 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
B:Co403

b:19.2
occ:1.00
OD2 B:ASP44 2.0 18.2 1.0
O B:HOH495 2.0 22.9 1.0
OD1 B:ASP167 2.1 14.0 1.0
O B:HOH551 2.1 13.9 1.0
O B:ASP46 2.2 14.5 1.0
CG B:ASP44 3.0 21.9 1.0
CG B:ASP167 3.1 18.8 1.0
C B:ASP46 3.3 15.5 1.0
OD2 B:ASP167 3.3 18.6 1.0
OD1 B:ASP44 3.3 16.9 1.0
OS B:OS404 3.4 95.4 1.0
O B:HOH549 3.5 23.6 1.0
CA B:ASP46 3.9 16.7 1.0
N B:ASP46 3.9 16.8 1.0
OG B:SER168 3.9 21.2 1.0
OG1 B:THR48 4.0 17.3 1.0
O B:HOH430 4.0 17.4 1.0
OD2 B:ASP171 4.1 25.6 1.0
CB B:ASP46 4.1 16.1 1.0
O B:HOH548 4.1 31.1 1.0
CB B:ASP44 4.4 20.4 1.0
N B:ASP47 4.4 17.5 1.0
CB B:ASP167 4.4 16.0 1.0
CB B:ASP47 4.5 17.9 1.0
N B:ASP167 4.5 18.5 1.0
N B:SER168 4.7 20.0 1.0
C B:ILE45 4.7 18.5 1.0
CA B:ASP47 4.7 17.5 1.0
C B:ASP47 4.7 17.7 1.0
N B:THR48 4.8 16.3 1.0
O B:HOH442 4.8 20.6 1.0
CB B:SER168 4.9 20.0 1.0
CB B:THR48 4.9 17.5 1.0
CA B:ASP167 5.0 17.8 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: Sun Dec 13 10:35:53 2020

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