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Zinc in PDB 2agz: Crystal Structure of the Carbinolamine Intermediate in the Reductive Half-Reaction of Aromatic Amine Dehydrogenase (Aadh) with Tryptamine. F222 Form

Enzymatic activity of Crystal Structure of the Carbinolamine Intermediate in the Reductive Half-Reaction of Aromatic Amine Dehydrogenase (Aadh) with Tryptamine. F222 Form

All present enzymatic activity of Crystal Structure of the Carbinolamine Intermediate in the Reductive Half-Reaction of Aromatic Amine Dehydrogenase (Aadh) with Tryptamine. F222 Form:
1.4.99.4;

Protein crystallography data

The structure of Crystal Structure of the Carbinolamine Intermediate in the Reductive Half-Reaction of Aromatic Amine Dehydrogenase (Aadh) with Tryptamine. F222 Form, PDB code: 2agz was solved by L.Masgrau, A.Roujeinikova, L.O.Johannissen, P.Hothi, J.Basran, K.E.Ranaghan, A.J.Mulholland, M.J.Sutcliffe, N.S.Scrutton, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.60
Space group F 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 119.913, 157.337, 267.996, 90.00, 90.00, 90.00
R / Rfree (%) 14.2 / 16.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Carbinolamine Intermediate in the Reductive Half-Reaction of Aromatic Amine Dehydrogenase (Aadh) with Tryptamine. F222 Form (pdb code 2agz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Carbinolamine Intermediate in the Reductive Half-Reaction of Aromatic Amine Dehydrogenase (Aadh) with Tryptamine. F222 Form, PDB code: 2agz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2agz

Go back to Zinc Binding Sites List in 2agz
Zinc binding site 1 out of 2 in the Crystal Structure of the Carbinolamine Intermediate in the Reductive Half-Reaction of Aromatic Amine Dehydrogenase (Aadh) with Tryptamine. F222 Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Carbinolamine Intermediate in the Reductive Half-Reaction of Aromatic Amine Dehydrogenase (Aadh) with Tryptamine. F222 Form within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn301

b:15.3
occ:0.50
ND1 D:HIS114 2.0 15.3 1.0
OD1 D:ASP121 2.0 12.8 1.0
CG D:ASP121 2.8 14.3 1.0
CE1 D:HIS114 3.0 16.7 1.0
CG D:HIS114 3.0 13.0 1.0
OD2 D:ASP121 3.0 20.2 1.0
CB D:HIS114 3.3 13.4 1.0
CA D:HIS114 4.0 15.4 1.0
NE2 D:HIS114 4.1 15.7 1.0
CD2 D:HIS114 4.1 18.1 1.0
CB D:ASP121 4.1 16.8 1.0
N D:ASP121 4.3 14.6 1.0
CA D:ASP121 4.5 13.9 1.0
C D:LYS120 4.7 16.3 1.0
N D:HIS114 4.7 15.5 1.0
O D:LYS120 5.0 15.3 1.0

Zinc binding site 2 out of 2 in 2agz

Go back to Zinc Binding Sites List in 2agz
Zinc binding site 2 out of 2 in the Crystal Structure of the Carbinolamine Intermediate in the Reductive Half-Reaction of Aromatic Amine Dehydrogenase (Aadh) with Tryptamine. F222 Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Carbinolamine Intermediate in the Reductive Half-Reaction of Aromatic Amine Dehydrogenase (Aadh) with Tryptamine. F222 Form within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Zn300

b:20.4
occ:0.40
ND1 H:HIS114 2.0 27.9 1.0
OD1 H:ASP121 2.0 20.5 1.0
CG H:ASP121 2.8 33.4 1.0
CE1 H:HIS114 3.0 39.3 1.0
OD2 H:ASP121 3.0 32.5 1.0
CG H:HIS114 3.0 29.0 1.0
CB H:HIS114 3.4 24.8 1.0
NE2 H:HIS114 4.1 41.0 1.0
CD2 H:HIS114 4.1 38.9 1.0
CA H:HIS114 4.1 23.9 1.0
CB H:ASP121 4.1 25.7 1.0
O H:HOH335 4.2 32.5 0.5
N H:ASP121 4.4 27.7 1.0
CA H:ASP121 4.6 21.7 1.0
O H:HOH393 4.6 43.1 1.0
O H:GLY119 4.7 39.7 1.0
C H:LYS120 4.8 29.2 1.0
N H:HIS114 5.0 22.0 1.0

Reference:

L.Masgrau, A.Roujeinikova, L.O.Johannissen, P.Hothi, J.Basran, K.E.Ranaghan, A.J.Mulholland, M.J.Sutcliffe, N.S.Scrutton, D.Leys. Atomic Description of An Enzyme Reaction Dominated By Proton Tunneling Science V. 312 237 2006.
ISSN: ISSN 0036-8075
PubMed: 16614214
DOI: 10.1126/SCIENCE.1126002
Page generated: Wed Oct 16 21:38:55 2024

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