Iron in PDB 1zzq: Rat Nnos D597N Mutant with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound

All present enzymatic activity of Rat Nnos D597N Mutant with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound:
1.14.13.39;

The structure of Rat Nnos D597N Mutant with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound, PDB code: 1zzq was solved by H.Li, M.L.Flinspach, J.Igarashi, J.Jamal, W.Yang, J.A.Gomez-Vidal, E.A.Litzinger, R.B.Silverman, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.89 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.860, 110.320, 164.600, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 24.4

The structure of Rat Nnos D597N Mutant with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Iron atom in the Rat Nnos D597N Mutant with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound (pdb code 1zzq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Rat Nnos D597N Mutant with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound, PDB code: 1zzq:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Rat Nnos D597N Mutant with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Rat Nnos D597N Mutant with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe750 b:22.7 occ:1.00 FE A:HEM750 0.0 22.7 1.0 NA A:HEM750 2.0 24.3 1.0 NC A:HEM750 2.0 23.7 1.0 ND A:HEM750 2.0 23.9 1.0 NB A:HEM750 2.0 24.0 1.0 SG A:CYS415 2.3 24.1 1.0 C1A A:HEM750 3.0 24.1 1.0 C4C A:HEM750 3.0 23.5 1.0 C1C A:HEM750 3.0 23.7 1.0 C1D A:HEM750 3.1 23.5 1.0 C4D A:HEM750 3.1 23.6 1.0 C4A A:HEM750 3.1 24.2 1.0 C1B A:HEM750 3.1 23.8 1.0 C4B A:HEM750 3.1 23.8 1.0 CB A:CYS415 3.3 23.7 1.0 CHD A:HEM750 3.4 23.7 1.0 CHA A:HEM750 3.4 23.6 1.0 CHC A:HEM750 3.5 23.9 1.0 CHB A:HEM750 3.5 23.9 1.0 CA A:CYS415 4.1 23.6 1.0 NH1 A:DP9799 4.2 35.3 0.5 C2A A:HEM750 4.3 24.4 1.0 C3C A:HEM750 4.3 23.6 1.0 C2D A:HEM750 4.3 23.5 1.0 C2C A:HEM750 4.3 24.0 1.0 C3D A:HEM750 4.3 23.6 1.0 C3A A:HEM750 4.3 24.6 1.0 C2B A:HEM750 4.3 24.1 1.0 C3B A:HEM750 4.4 23.9 1.0 NE1 A:TRP409 4.5 23.2 1.0 NH1 A:DP9799 4.5 34.5 0.5 NO A:DP9799 4.5 34.5 0.5 CZ A:DP9799 4.5 35.8 0.5 NO A:DP9799 4.5 35.1 0.5 CZ A:DP9799 4.7 35.0 0.5 O2 A:DP9799 4.7 34.6 0.5 O3 A:DP9799 4.8 34.1 0.5 C A:CYS415 4.8 23.3 1.0 NH2 A:DP9799 4.9 35.2 0.5 N A:GLY417 4.9 23.8 1.0 O2 A:DP9799 4.9 35.2 0.5 N A:VAL416 5.0 23.5 1.0 NH2 A:DP9799 5.0 34.5 0.5 O3 A:DP9799 5.0 34.9 0.5

Iron binding site 2 out of 2 in the Rat Nnos D597N Mutant with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Rat Nnos D597N Mutant with L-N(Omega)-Nitroarginine-(4R)- Amino-L-Proline Amide Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe750 b:20.1 occ:1.00 FE B:HEM750 0.0 20.1 1.0 NC B:HEM750 2.0 21.4 1.0 NB B:HEM750 2.0 21.9 1.0 ND B:HEM750 2.0 21.5 1.0 NA B:HEM750 2.0 21.5 1.0 SG B:CYS415 2.2 21.3 1.0 C4B B:HEM750 3.0 22.4 1.0 C1C B:HEM750 3.0 21.8 1.0 C4C B:HEM750 3.0 21.5 1.0 C1D B:HEM750 3.1 21.3 1.0 C1B B:HEM750 3.1 22.0 1.0 C4D B:HEM750 3.1 21.4 1.0 C1A B:HEM750 3.1 21.5 1.0 C4A B:HEM750 3.1 21.9 1.0 CB B:CYS415 3.3 20.1 1.0 CHC B:HEM750 3.4 22.1 1.0 CHD B:HEM750 3.4 21.7 1.0 CHA B:HEM750 3.4 21.3 1.0 CHB B:HEM750 3.5 22.0 1.0 NH1 B:DP9800 4.1 35.8 0.5 CA B:CYS415 4.1 20.3 1.0 C2C B:HEM750 4.3 21.8 1.0 C3B B:HEM750 4.3 22.8 1.0 C2B B:HEM750 4.3 22.4 1.0 C3C B:HEM750 4.3 21.9 1.0 C3D B:HEM750 4.3 22.1 1.0 C2D B:HEM750 4.3 21.8 1.0 C2A B:HEM750 4.3 22.2 1.0 C3A B:HEM750 4.4 21.7 1.0 NE1 B:TRP409 4.4 19.1 1.0 NO B:DP9800 4.4 34.0 0.5 NO B:DP9800 4.4 35.5 0.5 O2 B:DP9800 4.5 34.2 0.5 NH1 B:DP9800 4.5 34.1 0.5 CZ B:DP9800 4.5 36.1 0.5 CZ B:DP9800 4.6 34.5 0.5 O2 B:DP9800 4.7 35.8 0.5 N B:GLY417 4.8 20.6 1.0 C B:CYS415 4.8 20.5 1.0 O3 B:DP9800 4.9 33.8 0.5 NH2 B:DP9800 4.9 34.2 0.5 NH2 B:DP9800 4.9 35.6 0.5 N B:VAL416 5.0 20.2 1.0

H.Li, M.L.Flinspach, J.Igarashi, J.Jamal, W.Yang, E.A.Litzinger, H.Huang, E.P.Erdal, R.B.Silverman, T.L.Poulos. Exploring the Binding Conformations of Bulkier Dipeptide Amide Inhibitors in Constitutive Nitric Oxide Synthases. Biochemistry V. 44 15222 2005.
ISSN: ISSN 0006-2960
PubMed: 16285725
DOI: 10.1021/BI0513610