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Manganese in PDB 3n5u: Crystal Structure of An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1

Enzymatic activity of Crystal Structure of An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1

All present enzymatic activity of Crystal Structure of An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1:
3.1.3.16;

Protein crystallography data

The structure of Crystal Structure of An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1, PDB code: 3n5u was solved by A.M.Hirschi, M.Cecchini, R.C.Steinhardt, F.A.Dick, S.M.Rubin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 83.00 / 3.20
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 92.946, 92.946, 192.381, 90.00, 90.00, 90.00
R / Rfree (%) 22.1 / 26.1

Other elements in 3n5u:

The structure of Crystal Structure of An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1 also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1 (pdb code 3n5u). 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 An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1, PDB code: 3n5u:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 3n5u

Go back to Manganese Binding Sites List in 3n5u
Manganese binding site 1 out of 4 in the Crystal Structure of An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1


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 An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1

b:29.6
occ:1.00
 NE2 A:HIS66 2.3 39.0 1.0
OD2 A:ASP64 2.3 38.0 1.0
OD2 A:ASP92 2.3 36.7 1.0
MN A:MN2 3.0 27.0 1.0
CL A:CL301 3.0 45.2 1.0
CD2 A:HIS66 3.1 41.2 1.0
OH A:TYR272 3.2 50.3 1.0
CE1 A:HIS66 3.2 39.5 1.0
CG A:ASP92 3.5 38.6 1.0
CG A:ASP64 3.5 40.7 1.0
CZ A:TYR272 4.0 51.3 1.0
O A:HIS248 4.0 36.0 1.0
CB A:ASP92 4.1 39.8 1.0
CD2 A:HIS125 4.1 41.5 1.0
CB A:ASP64 4.2 41.8 1.0
CG A:HIS66 4.3 37.7 1.0
ND1 A:HIS66 4.3 38.1 1.0
OD1 A:ASP64 4.4 41.5 1.0
OD1 A:ASP92 4.4 36.2 1.0
NE2 A:HIS125 4.4 41.3 1.0
NH2 A:ARG96 4.5 48.3 1.0
CE2 A:TYR272 4.5 51.4 1.0
C A:HIS248 4.6 39.0 1.0
CE1 A:PHE267 4.6 45.5 1.0
CA A:HIS248 4.7 37.7 1.0
CE1 A:HIS173 4.7 37.0 1.0
NE2 A:HIS173 4.7 34.3 1.0
CE1 A:TYR272 4.8 56.4 1.0
ND1 A:HIS248 4.9 38.1 1.0

Manganese binding site 2 out of 4 in 3n5u

Go back to Manganese Binding Sites List in 3n5u
Manganese binding site 2 out of 4 in the Crystal Structure of An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1


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 An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn2

b:27.0
occ:1.00
 OD2 A:ASP92 2.2 36.7 1.0
ND1 A:HIS248 2.3 38.1 1.0
OD1 A:ASN124 2.4 33.3 1.0
NE2 A:HIS173 2.4 34.3 1.0
MN A:MN1 3.0 29.6 1.0
CE1 A:HIS248 3.0 39.0 1.0
CE1 A:HIS173 3.2 37.0 1.0
CG A:ASP92 3.2 38.6 1.0
CG A:ASN124 3.2 35.7 1.0
CL A:CL301 3.2 45.2 1.0
ND2 A:ASN124 3.3 35.0 1.0
CG A:HIS248 3.5 37.4 1.0
CD2 A:HIS173 3.5 37.2 1.0
OD1 A:ASP92 3.6 36.2 1.0
CA A:HIS248 3.6 37.7 1.0
OD2 A:ASP64 3.7 38.0 1.0
O A:HIS248 3.7 36.0 1.0
CB A:HIS248 4.0 38.6 1.0
C A:HIS248 4.1 39.0 1.0
CD2 A:HIS125 4.1 41.5 1.0
NE2 A:HIS248 4.2 36.9 1.0
ND1 A:HIS173 4.4 38.3 1.0
CD2 A:HIS248 4.4 37.6 1.0
CB A:ASP92 4.5 39.8 1.0
NE2 A:HIS66 4.5 39.0 1.0
CG A:ASP64 4.6 40.7 1.0
CG A:HIS173 4.6 36.1 1.0
N A:HIS248 4.6 35.8 1.0
CB A:ASN124 4.7 35.3 1.0
OD1 A:ASP64 4.7 41.5 1.0
NE2 A:HIS125 4.7 41.3 1.0
N A:ASN124 4.8 39.1 1.0
NH1 A:ARG221 4.8 41.4 1.0

Manganese binding site 3 out of 4 in 3n5u

Go back to Manganese Binding Sites List in 3n5u
Manganese binding site 3 out of 4 in the Crystal Structure of An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1


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 An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn3

b:30.6
occ:1.00
 OD2 B:ASP64 2.2 40.2 1.0
OD2 B:ASP92 2.3 37.4 1.0
NE2 B:HIS66 2.4 39.4 1.0
MN B:MN4 2.9 30.1 1.0
CD2 B:HIS66 3.2 42.7 1.0
OH B:TYR272 3.3 51.8 1.0
CE1 B:HIS66 3.4 39.7 1.0
CG B:ASP64 3.4 42.4 1.0
CG B:ASP92 3.5 39.9 1.0
CL B:CL2 3.5 39.4 1.0
O B:HIS248 3.9 37.2 1.0
CZ B:TYR272 4.1 52.6 1.0
CB B:ASP92 4.1 41.6 1.0
CB B:ASP64 4.2 42.1 1.0
CD2 B:HIS125 4.2 41.4 1.0
OD1 B:ASP64 4.3 41.5 1.0
CG B:HIS66 4.4 39.2 1.0
ND1 B:HIS66 4.4 39.3 1.0
OD1 B:ASP92 4.4 37.2 1.0
C B:HIS248 4.4 39.4 1.0
NE2 B:HIS125 4.5 42.6 1.0
CE1 B:PHE267 4.5 46.2 1.0
NH2 B:ARG96 4.5 47.0 1.0
CA B:HIS248 4.6 38.3 1.0
CE2 B:TYR272 4.6 51.7 1.0
CE1 B:HIS173 4.6 38.0 1.0
NE2 B:HIS173 4.6 36.4 1.0
ND1 B:HIS248 4.9 38.4 1.0
CE1 B:TYR272 4.9 57.0 1.0

Manganese binding site 4 out of 4 in 3n5u

Go back to Manganese Binding Sites List in 3n5u
Manganese binding site 4 out of 4 in the Crystal Structure of An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1


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 An Rb C-Terminal Peptide Bound to the Catalytic Subunit of PP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn4

b:30.1
occ:1.00
 OD2 B:ASP92 2.2 37.4 1.0
ND1 B:HIS248 2.3 38.4 1.0
OD1 B:ASN124 2.3 33.9 1.0
NE2 B:HIS173 2.4 36.4 1.0
MN B:MN3 2.9 30.6 1.0
CE1 B:HIS248 3.0 40.1 1.0
CL B:CL2 3.0 39.4 1.0
CG B:ASN124 3.2 36.1 1.0
CG B:ASP92 3.2 39.9 1.0
CE1 B:HIS173 3.2 38.0 1.0
ND2 B:ASN124 3.3 34.7 1.0
CG B:HIS248 3.5 37.6 1.0
OD1 B:ASP92 3.5 37.2 1.0
CD2 B:HIS173 3.6 37.2 1.0
CA B:HIS248 3.6 38.3 1.0
OD2 B:ASP64 3.7 40.2 1.0
O B:HIS248 3.7 37.2 1.0
CB B:HIS248 4.0 38.0 1.0
CD2 B:HIS125 4.1 41.4 1.0
C B:HIS248 4.1 39.4 1.0
NE2 B:HIS248 4.2 37.9 1.0
ND1 B:HIS173 4.4 39.2 1.0
CD2 B:HIS248 4.5 38.2 1.0
CB B:ASP92 4.5 41.6 1.0
NE2 B:HIS66 4.5 39.4 1.0
CG B:ASP64 4.6 42.4 1.0
CG B:HIS173 4.6 36.6 1.0
CB B:ASN124 4.6 35.0 1.0
N B:HIS248 4.7 37.8 1.0
NE2 B:HIS125 4.7 42.6 1.0
OD1 B:ASP64 4.8 41.5 1.0
N B:ASN124 4.8 38.4 1.0
NH1 B:ARG221 4.8 42.4 1.0

Reference:

A.Hirschi, M.Cecchini, R.C.Steinhardt, M.R.Schamber, F.A.Dick, S.M.Rubin. An Overlapping Kinase and Phosphatase Docking Site Regulates Activity of the Retinoblastoma Protein. Nat.Struct.Mol.Biol. V. 17 1051 2010.
ISSN: ISSN 1545-9993
PubMed: 20694007
DOI: 10.1038/NSMB.1868
Page generated: Sat Oct 5 17:17:03 2024

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