Iron in PDB 8t1k: Dsbu Crosslinked Nnos-Cam Oxygenase Homodimer

All present enzymatic activity of Dsbu Crosslinked Nnos-Cam Oxygenase Homodimer:
1.14.13.39;

The structure of Dsbu Crosslinked Nnos-Cam Oxygenase Homodimer also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Iron atom in the Dsbu Crosslinked Nnos-Cam Oxygenase Homodimer (pdb code 8t1k). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Dsbu Crosslinked Nnos-Cam Oxygenase Homodimer, PDB code: 8t1k:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Dsbu Crosslinked Nnos-Cam Oxygenase Homodimer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Dsbu Crosslinked Nnos-Cam Oxygenase Homodimer within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1504 b:20.0 occ:1.00 FE A:HEM1504 0.0 20.0 1.0 ND A:HEM1504 1.9 20.0 1.0 NB A:HEM1504 2.0 20.0 1.0 NA A:HEM1504 2.1 20.0 1.0 NC A:HEM1504 2.2 20.0 1.0 SG A:CYS415 2.2 0.0 1.0 C1D A:HEM1504 3.0 20.0 1.0 C4D A:HEM1504 3.0 20.0 1.0 C4B A:HEM1504 3.1 20.0 1.0 C1B A:HEM1504 3.1 20.0 1.0 C4A A:HEM1504 3.1 20.0 1.0 C1A A:HEM1504 3.1 20.0 1.0 C4C A:HEM1504 3.2 20.0 1.0 C1C A:HEM1504 3.2 20.0 1.0 CB A:CYS415 3.4 0.0 1.0 CHA A:HEM1504 3.4 20.0 1.0 CHD A:HEM1504 3.4 20.0 1.0 CHB A:HEM1504 3.4 20.0 1.0 CHC A:HEM1504 3.5 20.0 1.0 C2D A:HEM1504 4.2 20.0 1.0 C3D A:HEM1504 4.2 20.0 1.0 CA A:CYS415 4.2 0.0 1.0 NE1 A:TRP409 4.3 0.0 1.0 C2B A:HEM1504 4.3 20.0 1.0 C3B A:HEM1504 4.3 20.0 1.0 C3A A:HEM1504 4.3 20.0 1.0 C2A A:HEM1504 4.3 20.0 1.0 C2C A:HEM1504 4.4 20.0 1.0 C3C A:HEM1504 4.4 20.0 1.0 NH2 A:ARG1502 4.6 20.0 1.0 N A:GLY417 4.8 0.0 1.0 CZ A:ARG1502 4.9 20.0 1.0 CD1 A:TRP409 4.9 0.0 1.0 C A:CYS415 5.0 0.0 1.0

Iron binding site 2 out of 2 in the Dsbu Crosslinked Nnos-Cam Oxygenase Homodimer


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Dsbu Crosslinked Nnos-Cam Oxygenase Homodimer within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1503 b:20.0 occ:1.00 FE B:HEM1503 0.0 20.0 1.0 NB B:HEM1503 2.0 20.0 1.0 ND B:HEM1503 2.0 20.0 1.0 NA B:HEM1503 2.1 20.0 1.0 NC B:HEM1503 2.1 20.0 1.0 SG B:CYS415 2.8 0.0 1.0 C1D B:HEM1503 3.0 20.0 1.0 C1B B:HEM1503 3.0 20.0 1.0 C4B B:HEM1503 3.1 20.0 1.0 C4A B:HEM1503 3.1 20.0 1.0 C4D B:HEM1503 3.1 20.0 1.0 C1A B:HEM1503 3.1 20.0 1.0 C4C B:HEM1503 3.1 20.0 1.0 C1C B:HEM1503 3.2 20.0 1.0 CHD B:HEM1503 3.4 20.0 1.0 CHB B:HEM1503 3.4 20.0 1.0 CB B:CYS415 3.4 0.0 1.0 CHA B:HEM1503 3.5 20.0 1.0 CHC B:HEM1503 3.5 20.0 1.0 CA B:CYS415 4.2 0.0 1.0 NE1 B:TRP409 4.2 0.0 1.0 NH1 B:ARG1501 4.2 20.0 1.0 C2B B:HEM1503 4.2 20.0 1.0 C2D B:HEM1503 4.3 20.0 1.0 C3B B:HEM1503 4.3 20.0 1.0 C3D B:HEM1503 4.3 20.0 1.0 C3A B:HEM1503 4.3 20.0 1.0 C2A B:HEM1503 4.3 20.0 1.0 C3C B:HEM1503 4.4 20.0 1.0 C2C B:HEM1503 4.5 20.0 1.0 CZ B:ARG1501 4.6 20.0 1.0 N B:GLY417 4.8 0.0 1.0 CD1 B:TRP409 4.9 0.0 1.0 C B:CYS415 4.9 0.0 1.0

D.Felker, K.Lee, T.H.Pospiech, Y.Morishima, H.Zhang, M.Lau, D.Southworth, Y.Osawa. Mapping Interactions of Calmodulin and Neuronal No Synthase By Crosslinking and Mass Spectrometry. J.Biol.Chem. 05464 2023.
ISSN: ESSN 1083-351X
PubMed: 37979917
DOI: 10.1016/J.JBC.2023.105464