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Aluminium in PDB 2d33: Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride

Enzymatic activity of Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride

All present enzymatic activity of Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride:
6.3.2.2;

Protein crystallography data

The structure of Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride, PDB code: 2d33 was solved by T.Hibi, M.Nakayama, H.Nii, Y.Kurokawa, H.Katano, J.Oda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.60
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 325.226, 325.226, 105.181, 90.00, 90.00, 120.00
R / Rfree (%) 16.2 / 19.1

Other elements in 2d33:

The structure of Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride also contains other interesting chemical elements:

Fluorine (F) 12 atoms
Magnesium (Mg) 13 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride (pdb code 2d33). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 4 binding sites of Aluminium where determined in the Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride, PDB code: 2d33:
Jump to Aluminium binding site number: 1; 2; 3; 4;

Aluminium binding site 1 out of 4 in 2d33

Go back to Aluminium Binding Sites List in 2d33
Aluminium binding site 1 out of 4 in the Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al522

b:55.6
occ:1.00
 AL A:AF3522 0.0 55.6 1.0
F2 A:AF3522 1.6 51.6 1.0
F3 A:AF3522 1.8 49.7 1.0
F1 A:AF3522 1.8 52.0 1.0
O1B A:ADP521 2.4 33.9 1.0
MG A:MG525 2.5 26.8 1.0
MG A:MG523 3.0 40.9 1.0
OE2 A:GLU519 3.0 71.5 1.0
O A:HOH560 3.4 25.1 1.0
N A:CYS520 3.5 52.9 1.0
PB A:ADP521 3.7 33.3 1.0
MG A:MG524 3.7 34.6 1.0
OE1 A:GLU27 3.9 30.1 1.0
OE1 A:GLU67 4.0 34.9 1.0
OD1 A:ASP60 4.0 37.3 1.0
O2B A:ADP521 4.1 33.8 1.0
CD A:GLU519 4.2 71.2 1.0
OE2 A:GLU67 4.2 34.2 1.0
O A:HOH700 4.4 43.0 1.0
O2A A:ADP521 4.4 34.5 1.0
O3B A:ADP521 4.4 30.9 1.0
CD A:GLU67 4.6 32.0 1.0
OE1 A:GLU519 4.7 71.4 1.0
CA A:CYS520 4.7 53.3 1.0
O3A A:ADP521 4.8 32.5 1.0
CE1 A:HIS150 5.0 25.5 1.0

Aluminium binding site 2 out of 4 in 2d33

Go back to Aluminium Binding Sites List in 2d33
Aluminium binding site 2 out of 4 in the Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Al1522

b:60.7
occ:1.00
 AL B:AF31522 0.0 60.7 1.0
F2 B:AF31522 1.6 59.6 1.0
F3 B:AF31522 1.8 58.3 1.0
F1 B:AF31522 1.8 58.0 1.0
O1B B:ADP1521 2.2 38.8 1.0
MG B:MG1525 2.6 37.8 1.0
OE2 B:GLU1519 3.0 51.0 1.0
MG B:MG1523 3.1 45.8 1.0
PB B:ADP1521 3.2 36.7 1.0
OE1 B:GLU27 3.3 36.7 1.0
MG B:MG1524 3.3 36.4 1.0
O3B B:ADP1521 3.7 37.7 1.0
O B:HOH1589 3.7 44.1 1.0
O B:HOH1591 3.8 47.7 1.0
CD B:GLU1519 3.8 51.1 1.0
O2B B:ADP1521 3.9 37.2 1.0
N B:CYS1520 3.9 48.0 1.0
OD1 B:ASP60 4.0 43.1 1.0
OE1 B:GLU1519 4.0 50.0 1.0
O2A B:ADP1521 4.2 37.3 1.0
OE1 B:GLU67 4.3 38.7 1.0
OE2 B:GLU67 4.3 39.8 1.0
CD B:GLU27 4.4 35.6 1.0
O3A B:ADP1521 4.5 36.3 1.0
CE1 B:HIS150 4.7 31.1 1.0
CD B:GLU67 4.7 38.1 1.0
OE2 B:GLU27 4.8 35.6 1.0
ND1 B:HIS150 4.8 30.3 1.0
O B:HOH1554 4.8 45.6 1.0
PA B:ADP1521 5.0 37.2 1.0

Aluminium binding site 3 out of 4 in 2d33

Go back to Aluminium Binding Sites List in 2d33
Aluminium binding site 3 out of 4 in the Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 3 of Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Al2522

b:62.6
occ:1.00
 AL C:AF32522 0.0 62.6 1.0
F2 C:AF32522 1.6 60.3 1.0
F3 C:AF32522 1.8 60.2 1.0
F1 C:AF32522 1.8 59.9 1.0
O1B C:ADP2521 2.1 42.2 1.0
MG C:MG2525 2.8 45.8 1.0
MG C:MG2524 3.1 47.3 1.0
OE2 C:GLU2519 3.1 67.2 1.0
PB C:ADP2521 3.2 41.6 1.0
MG C:MG2523 3.2 46.3 1.0
OE1 C:GLU27 3.4 39.9 1.0
O2B C:ADP2521 3.7 41.9 1.0
O3B C:ADP2521 3.8 42.0 1.0
N C:CYS2520 3.8 55.2 1.0
OE1 C:GLU2519 3.9 67.4 1.0
O C:HOH2552 3.9 46.4 1.0
CD C:GLU2519 3.9 67.6 1.0
O2A C:ADP2521 4.3 46.0 1.0
OE2 C:GLU67 4.3 44.1 1.0
OD1 C:ASP60 4.3 49.9 1.0
O3A C:ADP2521 4.5 43.3 1.0
CD C:GLU27 4.5 39.9 1.0
OE1 C:GLU67 4.5 45.0 1.0
CE1 C:HIS150 4.6 38.9 1.0
ND1 C:HIS150 4.7 38.5 1.0
CD C:GLU67 4.9 43.5 1.0
OE2 C:GLU27 4.9 40.2 1.0
OE2 C:GLU328 5.0 41.0 1.0
CA C:CYS2520 5.0 55.4 1.0

Aluminium binding site 4 out of 4 in 2d33

Go back to Aluminium Binding Sites List in 2d33
Aluminium binding site 4 out of 4 in the Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 4 of Crystal Structure of Gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Al3522

b:62.7
occ:1.00
 AL D:AF33522 0.0 62.7 1.0
F2 D:AF33522 1.7 58.8 1.0
F1 D:AF33522 1.8 58.8 1.0
F3 D:AF33522 1.8 57.0 1.0
O1B D:ADP3521 2.2 37.2 1.0
MG D:MG3525 2.5 37.6 1.0
MG D:MG3523 2.9 38.2 1.0
OE2 D:GLU3519 2.9 49.5 1.0
OE1 D:GLU27 3.3 33.1 1.0
PB D:ADP3521 3.3 37.0 1.0
O D:HOH3555 3.4 30.2 1.0
MG D:MG3524 3.4 35.6 1.0
O D:HOH3593 3.6 37.7 1.0
N D:CYS3520 3.7 53.0 1.0
OD1 D:ASP60 3.8 40.1 1.0
O3B D:ADP3521 3.9 36.8 1.0
CD D:GLU3519 3.9 49.3 1.0
OE2 D:GLU67 3.9 37.8 1.0
OE1 D:GLU3519 4.1 48.9 1.0
O2B D:ADP3521 4.1 37.4 1.0
OE1 D:GLU67 4.2 39.4 1.0
O2A D:ADP3521 4.3 37.4 1.0
CD D:GLU27 4.4 32.2 1.0
CD D:GLU67 4.5 37.8 1.0
O3A D:ADP3521 4.6 37.0 1.0
CE1 D:HIS150 4.7 34.1 1.0
ND1 D:HIS150 4.8 33.6 1.0
OE2 D:GLU27 4.9 33.4 1.0
CA D:CYS3520 4.9 53.6 1.0
OE2 D:GLU29 5.0 38.1 1.0

Reference:

T.Hibi, M.Nakayama, H.Nii, Y.Kurokawa, H.Katano, J.Oda. Structural Basis of Efficient Coupling Between Peptide Ligation and Atp Hydrolysis By Gamma-Gluatamylcysteine Synthetase To Be Published.
Page generated: Wed Jul 10 09:29:25 2024

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