Zinc in PDB 4zr1: Hydroxylase Domain of SCS7P

The structure of Hydroxylase Domain of SCS7P, PDB code: 4zr1 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)	47.79 / 2.60
Space group	I 21 3
Cell size a, b, c (Å), α, β, γ (°)	202.762, 202.762, 202.762, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 23.9

The binding sites of Zinc atom in the Hydroxylase Domain of SCS7P (pdb code 4zr1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Hydroxylase Domain of SCS7P, PDB code: 4zr1:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Hydroxylase Domain of SCS7P


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Hydroxylase Domain of SCS7P within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:81.1 occ:1.00 NE2 A:HIS349 2.0 69.9 1.0 NE2 A:HIS330 2.1 61.5 1.0 NE2 A:HIS345 2.2 81.0 1.0 NE2 A:HIS271 2.3 75.5 1.0 NE2 A:HIS326 2.3 72.2 1.0 CE1 A:HIS349 2.9 69.5 1.0 CE1 A:HIS345 3.0 72.3 1.0 CE1 A:HIS330 3.0 70.8 1.0 CD2 A:HIS349 3.1 78.0 1.0 CD2 A:HIS330 3.1 63.7 1.0 CD2 A:HIS326 3.2 73.8 1.0 CD2 A:HIS271 3.2 57.8 1.0 CE1 A:HIS271 3.3 68.2 1.0 CE1 A:HIS326 3.4 78.8 1.0 CD2 A:HIS345 3.4 72.3 1.0 ND1 A:HIS349 4.1 74.6 1.0 ND1 A:HIS330 4.2 70.9 1.0 ND1 A:HIS345 4.2 66.8 1.0 CG A:HIS349 4.2 72.5 1.0 CG A:HIS330 4.2 62.8 1.0 ND1 A:HIS271 4.4 74.0 1.0 CG A:HIS271 4.4 65.2 1.0 CG A:HIS326 4.4 66.8 1.0 CG A:HIS345 4.4 70.2 1.0 ND1 A:HIS326 4.4 78.8 1.0

Zinc binding site 2 out of 4 in the Hydroxylase Domain of SCS7P


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Hydroxylase Domain of SCS7P within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:84.5 occ:1.00 NE2 A:HIS249 2.1 75.8 1.0 NE2 A:HIS348 2.2 85.9 1.0 NE2 A:HIS268 2.2 74.7 1.0 NE2 A:HIS272 2.3 82.8 1.0 NE2 A:HIS244 2.3 73.2 1.0 CE1 A:HIS249 3.0 79.8 1.0 CD2 A:HIS268 3.0 62.8 1.0 CE1 A:HIS348 3.1 86.5 1.0 CD2 A:HIS249 3.1 80.8 1.0 CD2 A:HIS348 3.2 80.0 1.0 CE1 A:HIS268 3.2 74.9 1.0 CD2 A:HIS272 3.2 74.2 1.0 CD2 A:HIS244 3.2 68.7 1.0 CE1 A:HIS272 3.3 79.4 1.0 CE1 A:HIS244 3.3 64.7 1.0 ND1 A:HIS249 4.1 74.1 1.0 ND1 A:HIS348 4.2 83.0 1.0 CG A:HIS249 4.2 73.0 1.0 CG A:HIS268 4.2 64.6 1.0 CG A:HIS348 4.3 75.9 1.0 ND1 A:HIS268 4.3 71.5 1.0 ND1 A:HIS272 4.4 83.8 1.0 CG A:HIS272 4.4 80.0 1.0 CG A:HIS244 4.4 74.3 1.0 ND1 A:HIS244 4.4 76.1 1.0

Zinc binding site 3 out of 4 in the Hydroxylase Domain of SCS7P


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Hydroxylase Domain of SCS7P within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:82.0 occ:1.00 NE2 B:HIS349 2.1 85.6 1.0 NE2 B:HIS330 2.1 70.8 1.0 NE2 B:HIS345 2.2 84.0 1.0 NE2 B:HIS326 2.2 75.5 1.0 NE2 B:HIS271 2.3 74.6 1.0 CE1 B:HIS349 3.0 89.2 1.0 CE1 B:HIS330 3.1 69.8 1.0 CD2 B:HIS349 3.1 85.3 1.0 CD2 B:HIS326 3.1 75.5 1.0 CD2 B:HIS330 3.1 66.6 1.0 CE1 B:HIS345 3.1 79.4 1.0 CD2 B:HIS345 3.2 68.2 1.0 CE1 B:HIS271 3.3 66.2 1.0 CD2 B:HIS271 3.3 70.8 1.0 CE1 B:HIS326 3.3 71.4 1.0 ND1 B:HIS349 4.1 81.7 1.0 ND1 B:HIS330 4.2 70.3 1.0 CG B:HIS349 4.2 84.0 1.0 CG B:HIS330 4.2 64.7 1.0 ND1 B:HIS345 4.3 75.8 1.0 CG B:HIS326 4.3 71.0 1.0 CG B:HIS345 4.3 75.0 1.0 ND1 B:HIS326 4.4 76.3 1.0 ND1 B:HIS271 4.4 66.9 1.0 CG B:HIS271 4.4 62.0 1.0

Zinc binding site 4 out of 4 in the Hydroxylase Domain of SCS7P


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Hydroxylase Domain of SCS7P within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:82.4 occ:1.00 NE2 B:HIS249 2.1 68.5 1.0 NE2 B:HIS272 2.1 74.9 1.0 NE2 B:HIS348 2.3 81.6 1.0 NE2 B:HIS268 2.3 74.0 1.0 NE2 B:HIS244 2.4 76.1 1.0 CE1 B:HIS249 3.0 62.9 1.0 CE1 B:HIS272 3.1 71.7 1.0 CD2 B:HIS272 3.1 66.0 1.0 CE1 B:HIS348 3.1 83.5 1.0 CD2 B:HIS249 3.2 69.1 1.0 CD2 B:HIS268 3.2 64.8 1.0 CD2 B:HIS348 3.3 75.7 1.0 CE1 B:HIS268 3.3 69.0 1.0 CD2 B:HIS244 3.3 65.2 1.0 CE1 B:HIS244 3.4 74.3 1.0 ND1 B:HIS249 4.2 64.1 1.0 ND1 B:HIS272 4.2 72.1 1.0 CG B:HIS249 4.3 67.5 1.0 CG B:HIS272 4.3 57.7 1.0 ND1 B:HIS348 4.3 83.8 1.0 CG B:HIS268 4.4 65.1 1.0 ND1 B:HIS268 4.4 74.1 1.0 CG B:HIS348 4.4 76.9 1.0 CG B:HIS244 4.5 65.0 1.0 ND1 B:HIS244 4.5 70.4 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