Zinc in PDB 1kah: L-Histidinol Dehydrogenase (Hisd) Structure Complexed with L-Histidine (Product), Zn and Nad (Cofactor)

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

The structure of L-Histidinol Dehydrogenase (Hisd) Structure Complexed with L-Histidine (Product), Zn and Nad (Cofactor), PDB code: 1kah 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)	38.12 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.260, 109.090, 157.940, 90.00, 90.00, 90.00
R / Rfree (%)	25.2 / 28.6

The binding sites of Zinc atom in the L-Histidinol Dehydrogenase (Hisd) Structure Complexed with L-Histidine (Product), Zn and Nad (Cofactor) (pdb code 1kah). 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-Histidine (Product), Zn and Nad (Cofactor), PDB code: 1kah:
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-Histidine (Product), Zn 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-Histidine (Product), Zn and Nad (Cofactor) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:32.3 occ:1.00 ND1 A:HIS502 1.9 61.3 1.0 OD2 A:ASP360 2.2 34.2 1.0 NE2 B:HIS419 2.2 22.5 1.0 NE2 A:HIS262 2.3 39.0 1.0 N A:HIS502 2.3 63.9 1.0 CE1 A:HIS502 2.7 61.5 1.0 CE1 A:HIS262 2.9 40.9 1.0 CG A:ASP360 3.0 34.2 1.0 OE1 A:GLU356 3.0 45.1 1.0 CD2 B:HIS419 3.0 22.8 1.0 CG A:HIS502 3.0 62.5 1.0 CE1 B:HIS419 3.3 24.1 1.0 CA A:HIS502 3.3 64.0 1.0 CD2 A:HIS262 3.5 40.9 1.0 CB A:HIS502 3.6 63.0 1.0 OD1 A:ASP360 3.6 36.6 1.0 CB A:ASP360 3.8 32.7 1.0 NE2 A:HIS502 3.9 61.4 1.0 CD2 A:HIS502 4.0 61.8 1.0 CD A:GLU356 4.1 41.9 1.0 ND1 A:HIS262 4.2 42.0 1.0 CG B:HIS419 4.2 24.0 1.0 ND1 B:HIS419 4.3 23.2 1.0 CG A:HIS262 4.4 41.4 1.0 C A:HIS502 4.7 64.4 1.0 O A:SER258 4.7 26.1 1.0 OE2 A:GLU356 4.8 41.4 1.0

Zinc binding site 2 out of 2 in the L-Histidinol Dehydrogenase (Hisd) Structure Complexed with L-Histidine (Product), Zn 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-Histidine (Product), Zn and Nad (Cofactor) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:35.0 occ:1.00 OD2 B:ASP360 1.9 31.7 1.0 NE2 B:HIS262 2.0 43.4 1.0 NE2 A:HIS419 2.1 25.2 1.0 ND1 A:HIS503 2.3 48.3 1.0 CG B:ASP360 2.8 30.9 1.0 CE1 A:HIS503 2.9 48.3 1.0 CE1 B:HIS262 3.0 44.8 1.0 CE1 A:HIS419 3.0 22.4 1.0 CD2 B:HIS262 3.0 41.6 1.0 CD2 A:HIS419 3.1 25.0 1.0 N A:HIS503 3.1 48.0 0.0 OE2 B:GLU356 3.3 46.4 1.0 OD1 B:ASP360 3.4 32.4 1.0 CG A:HIS503 3.6 48.8 1.0 CB B:ASP360 3.9 30.7 1.0 ND1 B:HIS262 4.1 43.3 1.0 CA A:HIS503 4.1 48.0 0.0 ND1 A:HIS419 4.1 25.4 1.0 NE2 A:HIS503 4.2 47.7 1.0 CB A:HIS503 4.2 48.0 1.0 CG B:HIS262 4.2 41.7 1.0 CD B:GLU356 4.2 41.8 1.0 CG A:HIS419 4.2 25.5 1.0 CD2 A:HIS503 4.5 47.2 1.0 CG B:GLU356 4.6 35.8 1.0 O B:SER258 4.8 24.9 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