Zinc in PDB 1kar: L-Histidinol Dehydrogenase (Hisd) Structure Complexed with Histamine (Inhibitor), Zinc and Nad (Cofactor)

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

The structure of L-Histidinol Dehydrogenase (Hisd) Structure Complexed with Histamine (Inhibitor), Zinc and Nad (Cofactor), PDB code: 1kar 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)	38.84 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.340, 109.040, 157.940, 90.00, 90.00, 90.00
R / Rfree (%)	24.8 / 28.1

The binding sites of Zinc atom in the L-Histidinol Dehydrogenase (Hisd) Structure Complexed with Histamine (Inhibitor), Zinc and Nad (Cofactor) (pdb code 1kar). 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 Histamine (Inhibitor), Zinc and Nad (Cofactor), PDB code: 1kar:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the L-Histidinol Dehydrogenase (Hisd) Structure Complexed with Histamine (Inhibitor), 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 Histamine (Inhibitor), Zinc and Nad (Cofactor) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:29.2 occ:1.00 ND1 A:HSM502 2.1 49.1 1.0 OD2 A:ASP360 2.1 28.4 1.0 NE2 B:HIS419 2.1 24.1 1.0 NE2 A:HIS262 2.2 33.8 1.0 CG A:ASP360 2.9 29.6 1.0 CE1 A:HSM502 3.0 49.8 1.0 CE1 A:HIS262 3.0 36.2 1.0 CE1 B:HIS419 3.1 26.2 1.0 CD2 B:HIS419 3.1 24.6 1.0 CG A:HSM502 3.1 50.6 1.0 CD2 A:HIS262 3.2 35.0 1.0 OD1 A:ASP360 3.4 30.1 1.0 CB A:HSM502 3.5 51.5 1.0 CB A:ASP360 3.9 28.4 1.0 NE2 A:HSM502 4.1 49.5 1.0 ND1 B:HIS419 4.2 27.0 1.0 ND1 A:HIS262 4.2 37.4 1.0 CD2 A:HSM502 4.2 49.8 1.0 CG B:HIS419 4.2 25.5 1.0 CG A:HIS262 4.3 37.1 1.0 OE1 A:GLU356 4.4 34.1 1.0 CA A:HSM502 4.5 52.5 1.0 CD A:GLU356 4.5 32.5 1.0 CG A:GLU356 4.7 31.1 1.0 CD1 B:LEU416 4.9 28.3 1.0 O A:SER258 4.9 22.0 1.0 N A:HSM502 4.9 54.4 1.0

Zinc binding site 2 out of 2 in the L-Histidinol Dehydrogenase (Hisd) Structure Complexed with Histamine (Inhibitor), 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 Histamine (Inhibitor), Zinc and Nad (Cofactor) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:29.4 occ:1.00 NE2 B:HIS262 2.1 33.9 1.0 NE2 A:HIS419 2.1 21.5 1.0 OD2 B:ASP360 2.1 27.0 1.0 ND1 B:HSM503 2.2 45.1 1.0 CG B:ASP360 2.9 28.0 1.0 CE1 B:HSM503 3.0 46.2 1.0 CD2 B:HIS262 3.0 30.7 1.0 CE1 A:HIS419 3.1 19.9 1.0 CD2 A:HIS419 3.1 19.8 1.0 CE1 B:HIS262 3.1 32.6 1.0 CG B:HSM503 3.4 46.1 1.0 OD1 B:ASP360 3.4 28.0 1.0 CB B:HSM503 3.9 45.8 1.0 CB B:ASP360 4.0 27.3 1.0 NE2 B:HSM503 4.2 46.0 1.0 ND1 A:HIS419 4.2 23.3 1.0 ND1 B:HIS262 4.2 32.0 1.0 CG B:HIS262 4.2 31.7 1.0 CG A:HIS419 4.2 21.1 1.0 CD2 B:HSM503 4.3 46.3 1.0 OE1 B:GLU356 4.5 35.1 1.0 CD B:GLU356 4.7 33.4 1.0 CG B:GLU356 4.8 28.7 1.0 CA B:HSM503 4.8 47.4 1.0 O B:SER258 4.8 23.1 1.0 CD1 A:LEU416 5.0 21.1 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