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Magnesium in PDB 2a2c: X-Ray Structure of Human N-Acetyl Galactosamine Kinase Complexed with Mg-Adp and N-Acetyl Galactosamine 1-Phosphate

Protein crystallography data

The structure of X-Ray Structure of Human N-Acetyl Galactosamine Kinase Complexed with Mg-Adp and N-Acetyl Galactosamine 1-Phosphate, PDB code: 2a2c was solved by J.B.Thoden, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.65
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 123.800, 123.800, 60.100, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 2a2c:

The structure of X-Ray Structure of Human N-Acetyl Galactosamine Kinase Complexed with Mg-Adp and N-Acetyl Galactosamine 1-Phosphate also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the X-Ray Structure of Human N-Acetyl Galactosamine Kinase Complexed with Mg-Adp and N-Acetyl Galactosamine 1-Phosphate (pdb code 2a2c). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the X-Ray Structure of Human N-Acetyl Galactosamine Kinase Complexed with Mg-Adp and N-Acetyl Galactosamine 1-Phosphate, PDB code: 2a2c:

Magnesium binding site 1 out of 1 in 2a2c

Go back to Magnesium Binding Sites List in 2a2c
Magnesium binding site 1 out of 1 in the X-Ray Structure of Human N-Acetyl Galactosamine Kinase Complexed with Mg-Adp and N-Acetyl Galactosamine 1-Phosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Structure of Human N-Acetyl Galactosamine Kinase Complexed with Mg-Adp and N-Acetyl Galactosamine 1-Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg460

b:9.4
occ:1.00
O A:HOH471 2.2 14.6 1.0
OP1 A:NG1459 2.2 19.1 1.0
O1B A:ADP463 2.3 15.0 1.0
O A:HOH470 2.3 14.1 1.0
O2A A:ADP463 2.3 14.8 1.0
OG A:SER147 2.4 13.1 1.0
PB A:ADP463 3.4 16.1 1.0
CB A:SER147 3.4 11.7 1.0
PA A:ADP463 3.6 17.1 1.0
P1 A:NG1459 3.6 27.6 1.0
O3A A:ADP463 3.8 17.0 1.0
O3B A:ADP463 3.9 18.1 1.0
OP2 A:NG1459 3.9 37.0 1.0
CE A:LYS234 4.2 18.4 1.0
OE2 A:GLU179 4.2 14.4 1.0
N A:SER147 4.3 15.0 1.0
O A:HOH472 4.3 13.7 1.0
O5' A:ADP463 4.4 17.4 1.0
O A:HOH473 4.4 14.9 1.0
CA A:SER147 4.4 12.6 1.0
CA A:SER145 4.4 14.1 1.0
OD2 A:ASP190 4.5 16.4 1.0
N2 A:NG1459 4.5 10.1 1.0
C8 A:NG1459 4.5 12.9 1.0
O1 A:NG1459 4.6 24.7 1.0
C7 A:NG1459 4.6 13.5 1.0
N A:SER148 4.6 14.2 1.0
OG A:SER148 4.7 14.2 1.0
OP3 A:NG1459 4.7 16.8 1.0
O2B A:ADP463 4.7 18.4 1.0
O A:HOH563 4.7 18.6 1.0
O1A A:ADP463 4.7 19.8 1.0
C A:SER145 4.8 17.1 1.0
C1 A:NG1459 4.9 13.7 1.0
C A:SER147 5.0 17.9 1.0

Reference:

J.B.Thoden, H.M.Holden. The Molecular Architecture of Human N-Acetylgalactosamine Kinase. J.Biol.Chem. V. 280 32784 2005.
ISSN: ISSN 0021-9258
PubMed: 16006554
DOI: 10.1074/JBC.M505730200
Page generated: Tue Aug 13 20:20:30 2024

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