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Manganese in PDB 1phk: Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product

Enzymatic activity of Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product

All present enzymatic activity of Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product:
2.7.1.38;

Protein crystallography data

The structure of Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product, PDB code: 1phk was solved by D.J.Owen, M.E.M.Noble, E.F.Garman, A.C.Papageorgiou, L.N.Johnson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.600, 67.400, 110.800, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 28.8

Manganese Binding Sites:

The binding sites of Manganese atom in the Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product (pdb code 1phk). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product, PDB code: 1phk:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1phk

Go back to Manganese Binding Sites List in 1phk
Manganese binding site 1 out of 2 in the Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn382

b:44.7
occ:1.00
O A:HOH446 2.2 49.9 1.0
OD1 A:ASP167 2.4 37.3 1.0
O2B A:ATP381 2.4 43.6 1.0
O3G A:ATP381 2.5 51.2 1.0
OD2 A:ASP167 2.5 35.3 1.0
CG A:ASP167 2.8 34.3 1.0
O3B A:ATP381 3.3 48.5 1.0
PG A:ATP381 3.4 59.1 1.0
PB A:ATP381 3.4 41.4 1.0
MN A:MN383 3.9 32.4 1.0
O2G A:ATP381 3.9 45.7 1.0
O A:HOH469 4.1 84.1 1.0
OD2 A:ASP149 4.2 38.7 1.0
CB A:ASP167 4.2 28.2 1.0
O1B A:ATP381 4.4 43.9 1.0
NZ A:LYS48 4.4 33.8 1.0
CA A:GLY169 4.4 24.5 1.0
O2A A:ATP381 4.5 42.3 1.0
O3A A:ATP381 4.5 31.9 1.0
N A:GLY169 4.6 23.1 1.0
O1G A:ATP381 4.6 54.6 1.0
PA A:ATP381 4.9 34.7 1.0
CE1 A:PHE170 5.0 32.0 1.0
CA A:ASP167 5.0 29.5 1.0

Manganese binding site 2 out of 2 in 1phk

Go back to Manganese Binding Sites List in 1phk
Manganese binding site 2 out of 2 in the Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn383

b:32.4
occ:1.00
OD1 A:ASN154 2.3 26.6 1.0
O2G A:ATP381 2.3 45.7 1.0
O2A A:ATP381 2.4 42.3 1.0
OD2 A:ASP167 2.4 35.3 1.0
O A:HOH403 2.5 37.7 1.0
O3B A:ATP381 2.6 48.5 1.0
PG A:ATP381 2.9 59.1 1.0
CG A:ASN154 3.3 27.1 1.0
CG A:ASP167 3.3 34.3 1.0
NZ A:LYS151 3.5 59.9 1.0
PA A:ATP381 3.6 34.7 1.0
O3G A:ATP381 3.7 51.2 1.0
ND2 A:ASN154 3.7 30.9 1.0
PB A:ATP381 3.8 41.4 1.0
CB A:ASP167 3.9 28.2 1.0
MN A:MN382 3.9 44.7 1.0
O3A A:ATP381 3.9 31.9 1.0
O2B A:ATP381 4.1 43.6 1.0
O1G A:ATP381 4.2 54.6 1.0
O A:HOH532 4.2 76.3 1.0
OD1 A:ASP167 4.3 37.3 1.0
O5' A:ATP381 4.6 46.0 1.0
C5' A:ATP381 4.6 36.1 1.0
O1A A:ATP381 4.6 34.4 1.0
CB A:ASN154 4.7 24.8 1.0
OD2 A:ASP149 4.7 38.7 1.0
CE A:LYS151 4.7 58.1 1.0
O3' A:ATP381 4.7 35.7 1.0
O A:GLU153 4.8 37.6 1.0
CA A:ASN154 5.0 29.3 1.0

Reference:

D.J.Owen, M.E.Noble, E.F.Garman, A.C.Papageorgiou, L.N.Johnson. Two Structures of the Catalytic Domain of Phosphorylase Kinase: An Active Protein Kinase Complexed with Substrate Analogue and Product. Structure V. 3 467 1995.
ISSN: ISSN 0969-2126
PubMed: 7663944
DOI: 10.1016/S0969-2126(01)00180-0
Page generated: Tue Dec 15 03:54:13 2020

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