Zinc in PDB 4zr0: Full Length SCS7P (Only Hydroxylase Domain Visible)

The structure of Full Length SCS7P (Only Hydroxylase Domain Visible), PDB code: 4zr0 was solved by G.Zhu, M.Koszelak-Rosenblum, M.G.Malkowski, Membrane Protein Structuralbiology Consortium (Mpsbc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.83 / 3.80
Space group	I 21 3
Cell size a, b, c (Å), α, β, γ (°)	202.943, 202.943, 202.943, 90.00, 90.00, 90.00
R / Rfree (%)	24.6 / 27.1

The binding sites of Zinc atom in the Full Length SCS7P (Only Hydroxylase Domain Visible) (pdb code 4zr0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Full Length SCS7P (Only Hydroxylase Domain Visible), PDB code: 4zr0:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Full Length SCS7P (Only Hydroxylase Domain Visible)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Full Length SCS7P (Only Hydroxylase Domain Visible) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:63.6 occ:1.00 NE2 A:HIS271 2.1 62.0 1.0 NE2 A:HIS349 2.1 65.4 1.0 NE2 A:HIS330 2.2 55.0 1.0 NE2 A:HIS326 2.3 58.7 1.0 NE2 A:HIS345 2.4 63.9 1.0 CE1 A:HIS349 2.9 65.0 1.0 CD2 A:HIS271 3.0 60.2 1.0 CE1 A:HIS330 3.0 55.7 1.0 CE1 A:HIS271 3.1 62.0 1.0 CD2 A:HIS349 3.1 67.2 1.0 CD2 A:HIS326 3.1 57.0 1.0 CD2 A:HIS330 3.2 56.2 1.0 CD2 A:HIS345 3.3 63.4 1.0 CE1 A:HIS326 3.4 58.0 1.0 CE1 A:HIS345 3.4 63.3 1.0 ND1 A:HIS349 4.1 65.7 1.0 CG A:HIS271 4.1 59.3 1.0 ND1 A:HIS271 4.1 60.1 1.0 CG A:HIS349 4.2 68.1 1.0 ND1 A:HIS330 4.2 57.1 1.0 CG A:HIS330 4.3 58.5 1.0 CG A:HIS326 4.3 55.5 1.0 ND1 A:HIS326 4.4 56.0 1.0 CG A:HIS345 4.4 62.6 1.0 ND1 A:HIS345 4.5 62.7 1.0 O A:HIS326 4.9 54.9 1.0

Zinc binding site 2 out of 4 in the Full Length SCS7P (Only Hydroxylase Domain Visible)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Full Length SCS7P (Only Hydroxylase Domain Visible) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:61.5 occ:1.00 NE2 A:HIS249 2.0 52.4 1.0 NE2 A:HIS348 2.1 76.4 1.0 NE2 A:HIS272 2.2 61.9 1.0 NE2 A:HIS268 2.3 59.2 1.0 NE2 A:HIS244 2.6 54.7 1.0 CE1 A:HIS249 2.7 53.3 1.0 CE1 A:HIS348 2.9 76.5 1.0 CE1 A:HIS272 3.0 62.1 1.0 CD2 A:HIS268 3.2 57.0 1.0 CD2 A:HIS249 3.2 53.1 1.0 CD2 A:HIS348 3.3 77.0 1.0 CD2 A:HIS272 3.3 62.5 1.0 CE1 A:HIS268 3.4 59.0 1.0 CD2 A:HIS244 3.5 52.0 1.0 CE1 A:HIS244 3.5 55.2 1.0 ND1 A:HIS249 3.9 54.2 1.0 ND1 A:HIS348 4.1 77.0 1.0 ND1 A:HIS272 4.2 62.5 1.0 CG A:HIS249 4.2 54.6 1.0 CG A:HIS348 4.3 76.6 1.0 CG A:HIS268 4.4 55.3 1.0 CG A:HIS272 4.4 62.8 1.0 ND1 A:HIS268 4.4 56.9 1.0 ND1 A:HIS244 4.6 53.8 1.0 CG A:HIS244 4.7 49.2 1.0

Zinc binding site 3 out of 4 in the Full Length SCS7P (Only Hydroxylase Domain Visible)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Full Length SCS7P (Only Hydroxylase Domain Visible) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:51.9 occ:1.00 NE2 B:HIS345 2.1 67.9 1.0 NE2 B:HIS330 2.1 63.4 1.0 NE2 B:HIS349 2.1 56.2 1.0 NE2 B:HIS271 2.2 57.0 1.0 NE2 B:HIS326 2.4 61.2 1.0 CD2 B:HIS345 2.9 67.9 1.0 CE1 B:HIS330 3.0 63.5 1.0 CD2 B:HIS349 3.0 58.4 1.0 CE1 B:HIS349 3.1 54.5 1.0 CD2 B:HIS330 3.1 64.7 1.0 CE1 B:HIS271 3.1 56.1 1.0 CD2 B:HIS326 3.1 62.5 1.0 CE1 B:HIS345 3.2 67.5 1.0 CD2 B:HIS271 3.2 54.4 1.0 CE1 B:HIS326 3.6 60.0 1.0 CG B:HIS345 4.1 67.2 1.0 ND1 B:HIS330 4.1 64.9 1.0 ND1 B:HIS349 4.1 55.1 1.0 CG B:HIS349 4.2 58.4 1.0 ND1 B:HIS345 4.2 67.5 1.0 CG B:HIS330 4.2 66.5 1.0 ND1 B:HIS271 4.2 52.8 1.0 CG B:HIS271 4.3 52.6 1.0 CG B:HIS326 4.4 61.0 1.0 ND1 B:HIS326 4.6 60.2 1.0 O B:HIS326 4.8 54.4 1.0

Zinc binding site 4 out of 4 in the Full Length SCS7P (Only Hydroxylase Domain Visible)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Full Length SCS7P (Only Hydroxylase Domain Visible) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:60.0 occ:1.00 NE2 B:HIS249 2.0 55.3 1.0 NE2 B:HIS348 2.1 71.5 1.0 NE2 B:HIS272 2.1 58.4 1.0 NE2 B:HIS268 2.4 55.5 1.0 NE2 B:HIS244 2.6 44.0 1.0 CE1 B:HIS249 2.8 54.6 1.0 CE1 B:HIS348 2.9 71.8 1.0 CE1 B:HIS272 3.0 60.6 1.0 CD2 B:HIS249 3.2 55.2 1.0 CD2 B:HIS268 3.2 53.2 1.0 CD2 B:HIS348 3.3 72.3 1.0 CD2 B:HIS272 3.3 56.5 1.0 CE1 B:HIS268 3.4 56.0 1.0 CE1 B:HIS244 3.5 47.2 1.0 CD2 B:HIS244 3.6 33.4 1.0 ND1 B:HIS249 4.0 53.5 1.0 ND1 B:HIS348 4.1 73.2 1.0 ND1 B:HIS272 4.1 59.8 1.0 CG B:HIS249 4.2 53.2 1.0 CG B:HIS348 4.3 72.4 1.0 CG B:HIS272 4.3 57.2 1.0 CG B:HIS268 4.4 51.7 1.0 ND1 B:HIS268 4.5 54.0 1.0 ND1 B:HIS244 4.6 49.4 1.0 CG B:HIS244 4.7 48.2 1.0

G.Zhu, M.Koszelak-Rosenblum, S.M.Connelly, M.E.Dumont, M.G.Malkowski. The Crystal Structure of An Integral Membrane Fatty Acid Alpha-Hydroxylase. J.Biol.Chem. V. 290 29820 2015.
ISSN: ESSN 1083-351X
PubMed: 26515067
DOI: 10.1074/JBC.M115.680124