Zinc in PDB 1kae: L-Histidinol Dehydrogenase (Hisd) Structure Complexed with L- Histidinol (Substrate), Zinc and Nad (Cofactor)

All present enzymatic activity of L-Histidinol Dehydrogenase (Hisd) Structure Complexed with L- Histidinol (Substrate), Zinc and Nad (Cofactor):
1.1.1.23;

The structure of L-Histidinol Dehydrogenase (Hisd) Structure Complexed with L- Histidinol (Substrate), Zinc and Nad (Cofactor), PDB code: 1kae was solved by J.A.R.G.Barbosa, J.Sivaraman, Y.Li, R.Larocque, A.Matte, J.D.Schrag, M.Cygler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.50 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.930, 107.940, 156.710, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 24.1

The binding sites of Zinc atom in the L-Histidinol Dehydrogenase (Hisd) Structure Complexed with L- Histidinol (Substrate), Zinc and Nad (Cofactor) (pdb code 1kae). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the L-Histidinol Dehydrogenase (Hisd) Structure Complexed with L- Histidinol (Substrate), Zinc and Nad (Cofactor), PDB code: 1kae:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the L-Histidinol Dehydrogenase (Hisd) Structure Complexed with L- Histidinol (Substrate), Zinc and Nad (Cofactor)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of L-Histidinol Dehydrogenase (Hisd) Structure Complexed with L- Histidinol (Substrate), Zinc and Nad (Cofactor) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1101 b:19.5 occ:1.00 ND1 A:HSO1001 2.0 15.8 1.0 NE2 B:HIS419 2.0 17.5 1.0 NE2 A:HIS262 2.1 14.3 1.0 OD2 A:ASP360 2.2 17.6 1.0 N A:HSO1001 2.2 20.6 1.0 OE1 A:GLN259 2.6 20.0 1.0 CE1 A:HSO1001 3.0 16.4 1.0 CE1 A:HIS262 3.0 17.2 1.0 CE1 B:HIS419 3.0 15.1 1.0 CG A:HSO1001 3.0 16.4 1.0 CD2 B:HIS419 3.0 16.5 1.0 CG A:ASP360 3.1 18.5 1.0 CA A:HSO1001 3.1 18.9 1.0 CD2 A:HIS262 3.2 18.0 1.0 CB A:HSO1001 3.4 16.4 1.0 CD A:GLN259 3.4 20.1 1.0 NE2 A:GLN259 3.6 19.8 1.0 OD1 A:ASP360 3.7 18.0 1.0 CB A:ASP360 4.0 18.5 1.0 NE2 A:HSO1001 4.1 17.4 1.0 OE1 A:GLU356 4.1 23.2 1.0 CD2 A:HSO1001 4.1 17.6 1.0 ND1 B:HIS419 4.1 15.0 1.0 ND1 A:HIS262 4.2 18.3 1.0 CG B:HIS419 4.2 17.1 1.0 OG A:SER237 4.3 26.4 1.0 CG A:HIS262 4.3 18.6 1.0 C A:HSO1001 4.5 19.7 1.0 O A:SER258 4.8 20.9 1.0 CG A:GLN259 4.9 17.9 1.0 CB A:SER237 5.0 24.5 1.0 O A:HSO1001 5.0 19.9 1.0

Zinc binding site 2 out of 2 in the L-Histidinol Dehydrogenase (Hisd) Structure Complexed with L- Histidinol (Substrate), Zinc and Nad (Cofactor)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of L-Histidinol Dehydrogenase (Hisd) Structure Complexed with L- Histidinol (Substrate), Zinc and Nad (Cofactor) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1102 b:21.5 occ:1.00 OD2 B:ASP360 2.0 22.2 1.0 NE2 A:HIS419 2.0 17.0 1.0 NE2 B:HIS262 2.1 20.7 1.0 N3 B:IMD902 2.1 17.5 1.0 O B:HOH1299 2.1 30.6 1.0 CG B:ASP360 2.8 21.9 1.0 CE1 B:HIS262 2.9 21.9 1.0 CE1 A:HIS419 3.0 14.7 1.0 C2 B:IMD902 3.0 18.4 1.0 CD2 A:HIS419 3.0 15.7 1.0 C4 B:IMD902 3.1 17.9 1.0 CD2 B:HIS262 3.2 21.6 1.0 OD1 B:ASP360 3.4 24.0 1.0 CB B:ASP360 3.9 20.4 1.0 O B:HOH1483 4.0 28.4 1.0 ND1 B:HIS262 4.1 21.8 1.0 ND1 A:HIS419 4.1 15.9 1.0 N1 B:IMD902 4.2 18.6 1.0 CG A:HIS419 4.2 15.8 1.0 OE2 B:GLU356 4.2 31.4 1.0 C5 B:IMD902 4.2 16.9 1.0 CG B:HIS262 4.2 23.4 1.0 O B:SER258 4.9 21.4 1.0 CG B:GLU356 4.9 27.7 1.0 CD B:GLU356 4.9 29.9 1.0

J.A.R.G.Barbosa, J.Sivaraman, Y.Li, R.Larocque, A.Matte, J.D.Schrag, M.Cygler. Mechanism of Action and Nad+-Binding Mode Revealed By the Crystal Structure of L-Histidinol Dehydrogenase. Proc.Natl.Acad.Sci.Usa V. 99 1859 2002.
ISSN: ISSN 0027-8424
PubMed: 11842181
DOI: 10.1073/PNAS.022476199