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Magnesium in PDB 1e19: Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase From the Hyperthermophilic Archaeon Pyrococcus Furiosus Bound to Adp

Enzymatic activity of Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase From the Hyperthermophilic Archaeon Pyrococcus Furiosus Bound to Adp

All present enzymatic activity of Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase From the Hyperthermophilic Archaeon Pyrococcus Furiosus Bound to Adp:
2.7.2.2;

Protein crystallography data

The structure of Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase From the Hyperthermophilic Archaeon Pyrococcus Furiosus Bound to Adp, PDB code: 1e19 was solved by S.Ramon-Maiques, A.Marina, M.Uriarte, I.Fita, V.Rubio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15 / 1.5
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.400, 91.700, 133.800, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 21.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase From the Hyperthermophilic Archaeon Pyrococcus Furiosus Bound to Adp (pdb code 1e19). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase From the Hyperthermophilic Archaeon Pyrococcus Furiosus Bound to Adp, PDB code: 1e19:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1e19

Go back to Magnesium Binding Sites List in 1e19
Magnesium binding site 1 out of 2 in the Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase From the Hyperthermophilic Archaeon Pyrococcus Furiosus Bound to Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase From the Hyperthermophilic Archaeon Pyrococcus Furiosus Bound to Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg316

b:25.3
occ:1.00
 O A:HOH2342 2.1 52.4 1.0
O2A A:ADP315 2.3 24.1 1.0
O A:HOH2344 2.4 30.3 1.0
O A:HOH2389 2.4 32.5 1.0
O3B A:ADP315 2.5 23.8 1.0
O A:HOH2391 2.5 26.2 1.0
PB A:ADP315 3.5 20.1 1.0
PA A:ADP315 3.5 21.6 1.0
O A:HOH2382 3.6 35.6 1.0
O3A A:ADP315 3.7 22.1 1.0
O A:HOH2278 3.8 23.2 1.0
O A:HOH2279 3.9 26.5 1.0
O1B A:ADP315 3.9 22.9 1.0
NZ A:LYS277 4.2 24.6 1.0
O A:HOH2161 4.2 48.2 1.0
O A:HOH2030 4.3 48.1 1.0
O5' A:ADP315 4.4 23.4 1.0
O A:GLY272 4.5 29.6 1.0
O1A A:ADP315 4.6 23.5 1.0
CE A:LYS277 4.7 23.2 1.0
CA A:SER273 4.7 25.9 1.0
O A:SER273 4.7 22.9 1.0
O2B A:ADP315 4.8 21.2 1.0
O A:HOH2390 4.9 33.5 1.0

Magnesium binding site 2 out of 2 in 1e19

Go back to Magnesium Binding Sites List in 1e19
Magnesium binding site 2 out of 2 in the Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase From the Hyperthermophilic Archaeon Pyrococcus Furiosus Bound to Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase From the Hyperthermophilic Archaeon Pyrococcus Furiosus Bound to Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg316

b:27.9
occ:1.00
 O1A B:ADP315 2.2 25.6 1.0
O B:HOH2323 2.4 28.6 1.0
O B:HOH2286 2.5 42.4 1.0
O3B B:ADP315 2.5 24.3 1.0
O B:HOH2288 2.5 31.6 1.0
O B:HOH2320 2.5 30.4 1.0
PA B:ADP315 3.4 23.4 1.0
PB B:ADP315 3.5 22.7 1.0
O3A B:ADP315 3.7 23.1 1.0
O B:HOH2321 3.8 40.6 1.0
O1B B:ADP315 3.8 23.8 1.0
O B:HOH2238 3.9 28.2 1.0
O B:HOH2236 3.9 25.8 1.0
NZ B:LYS277 4.1 27.4 1.0
O5' B:ADP315 4.3 24.4 1.0
O B:GLY272 4.4 34.5 1.0
O2A B:ADP315 4.5 25.9 1.0
NZ B:LYS215 4.6 29.4 0.5
CE B:LYS277 4.7 23.6 1.0
CA B:SER273 4.8 23.4 1.0
O B:SER273 4.8 23.1 1.0
O B:HOH2317 4.9 37.4 1.0
O2B B:ADP315 4.9 23.0 1.0

Reference:

S.Ramon-Maiques, A.Marina, M.Uriarte, I.Fita, V.Rubio. The 1.5-A Resolution Crystal Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase From the Hyperthermophilic Archaeon Pyrococcus Furiosus, Bound to Adp, Confirms That This Thermoestable Enzyme Is A Carbamate Kinase, and Provides Insights Into Substrate Binding and Stability in Carbamate Kinases J.Mol.Biol. V. 299 463 2000.
ISSN: ISSN 0022-2836
PubMed: 10860751
DOI: 10.1006/JMBI.2000.3779
Page generated: Tue Aug 13 02:48:31 2024

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