Zinc in PDB 9ey6: Crystal Structure of Human Tyrosinase-Related Protein 1 (TYRP1)

The structure of Crystal Structure of Human Tyrosinase-Related Protein 1 (TYRP1), PDB code: 9ey6 was solved by Y.M.Ng, M.Soler-Lopez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.97 / 2.23
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	103.754, 103.754, 140.988, 90, 90, 120
R / Rfree (%)	17 / 21.3

The binding sites of Zinc atom in the Crystal Structure of Human Tyrosinase-Related Protein 1 (TYRP1) (pdb code 9ey6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Crystal Structure of Human Tyrosinase-Related Protein 1 (TYRP1), PDB code: 9ey6:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in the Crystal Structure of Human Tyrosinase-Related Protein 1 (TYRP1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human Tyrosinase-Related Protein 1 (TYRP1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn506 b:34.1 occ:1.00 NE2 A:HIS192 2.0 29.4 1.0 NE2 A:HIS215 2.1 40.7 1.0 NE2 A:HIS224 2.1 31.4 1.0 O A:HOH716 2.2 28.3 1.0 CE1 A:HIS192 3.0 35.6 1.0 CE1 A:HIS215 3.0 43.2 1.0 CD2 A:HIS192 3.0 32.9 1.0 CE1 A:HIS224 3.0 31.6 1.0 CD2 A:HIS215 3.1 38.5 1.0 CD2 A:HIS224 3.2 34.0 1.0 ZN A:ZN507 3.6 35.0 1.0 CE2 A:PHE400 4.0 36.4 1.0 CZ A:PHE400 4.0 38.6 1.0 O A:HOH763 4.0 54.0 1.0 ND1 A:HIS192 4.1 31.3 1.0 ND1 A:HIS215 4.1 39.5 1.0 NE2 A:HIS404 4.1 33.6 1.0 CG A:HIS192 4.2 28.2 1.0 ND1 A:HIS224 4.2 27.1 1.0 CG A:HIS215 4.2 39.2 1.0 CG A:HIS224 4.3 30.5 1.0 O A:HOH698 4.3 50.5 1.0 CE1 A:HIS404 4.6 34.1 1.0 CE1 A:PHE220 4.9 36.6 1.0 NE2 A:HIS377 4.9 36.2 1.0 CD2 A:HIS404 5.0 31.0 1.0

Zinc binding site 2 out of 5 in the Crystal Structure of Human Tyrosinase-Related Protein 1 (TYRP1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Human Tyrosinase-Related Protein 1 (TYRP1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn507 b:35.0 occ:1.00 O A:HOH716 1.6 28.3 1.0 NE2 A:HIS404 2.0 33.6 1.0 NE2 A:HIS377 2.0 36.2 1.0 NE2 A:HIS381 2.1 39.4 1.0 CE1 A:HIS404 2.9 34.1 1.0 CD2 A:HIS377 3.0 37.7 1.0 CE1 A:HIS381 3.0 39.9 1.0 CD2 A:HIS404 3.0 31.0 1.0 CD2 A:HIS381 3.0 38.9 1.0 CE1 A:HIS377 3.1 36.8 1.0 ZN A:ZN506 3.6 34.1 1.0 O A:HOH763 3.9 54.0 1.0 CE2 A:PHE400 4.0 36.4 1.0 ND1 A:HIS404 4.0 31.2 1.0 ND1 A:HIS381 4.1 39.6 1.0 CG A:HIS404 4.1 33.9 1.0 CG A:HIS377 4.2 31.6 1.0 CG A:HIS381 4.2 36.7 1.0 ND1 A:HIS377 4.2 33.7 1.0 O A:HOH698 4.2 50.5 1.0 NE2 A:HIS224 4.3 31.4 1.0 CZ A:PHE400 4.5 38.6 1.0 CD2 A:HIS224 4.5 34.0 1.0 CD2 A:PHE400 4.6 37.4 1.0 CD2 A:LEU403 4.6 37.8 1.0 CE1 A:PHE220 4.6 36.6 1.0 CZ A:PHE220 4.9 33.2 1.0 NE2 A:HIS215 4.9 40.7 1.0

Zinc binding site 3 out of 5 in the Crystal Structure of Human Tyrosinase-Related Protein 1 (TYRP1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Human Tyrosinase-Related Protein 1 (TYRP1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn508 b:54.5 occ:1.00 NE2 A:HIS75 1.9 51.3 1.0 NE2 A:HIS81 2.0 95.3 1.0 OE2 A:GLU88 2.1 64.1 1.0 OE1 A:GLU88 2.2 65.9 1.0 CD A:GLU88 2.5 58.1 1.0 CE1 A:HIS75 2.9 58.3 1.0 CD2 A:HIS75 3.0 53.4 1.0 CD2 A:HIS81 3.0 84.2 1.0 CE1 A:HIS81 3.0 94.5 1.0 CG A:GLU88 4.0 59.6 1.0 ND1 A:HIS75 4.0 46.4 1.0 ND1 A:HIS81 4.1 101.8 1.0 CG A:HIS81 4.1 97.6 1.0 CG A:HIS75 4.1 51.9 1.0 CD1 A:ILE432 4.6 43.9 1.0 CA A:GLY83 4.6 87.3 1.0 OE1 A:GLN78 4.9 82.4 1.0

Zinc binding site 4 out of 5 in the Crystal Structure of Human Tyrosinase-Related Protein 1 (TYRP1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Human Tyrosinase-Related Protein 1 (TYRP1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn509 b:51.4 occ:1.00 OE2 A:GLU329 2.1 79.0 1.0 OE1 A:GLU329 2.2 66.5 1.0 CD A:GLU329 2.5 60.2 1.0 CG A:GLU329 4.0 59.8 1.0 NE A:ARG326 4.7 74.7 1.0

Zinc binding site 5 out of 5 in the Crystal Structure of Human Tyrosinase-Related Protein 1 (TYRP1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Human Tyrosinase-Related Protein 1 (TYRP1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn510 b:54.0 occ:0.50 O A:HOH615 1.9 65.6 1.0 OE2 A:GLU241 2.0 71.7 1.0 OE1 A:GLU241 2.1 69.4 1.0 CD A:GLU241 2.3 70.7 1.0 CE1 A:HIS143 2.4 63.0 1.0 O A:HOH605 2.6 73.0 1.0 O A:HOH770 2.8 67.3 1.0 ND1 A:HIS143 3.2 67.6 1.0 O1 A:GOL505 3.3 86.4 1.0 NE2 A:HIS143 3.4 69.7 1.0 CG A:GLU241 3.8 62.5 1.0 CG A:HIS143 4.4 63.5 1.0 CD2 A:HIS143 4.4 68.2 1.0 O A:HOH664 4.5 58.6 1.0 C1 A:GOL505 4.7 74.1 1.0 O A:HOH694 4.8 44.3 1.0 CB A:GLU241 5.0 52.9 1.0

C.Faure, Y.M.Ng, C.Belle, M.Soler-Lopez, L.Khettabi, M.Saidi, N.Berthet, M.Maresca, C.Philouze, W.Rachidi, M.Reglier, A.Du Moullinet D'hardemare, H.Jamet. Interactions of Phenylalanine Derivatives with Human Tyrosinase: Lessons From Experimental and Theoretical Studies. Chembiochem 00235 2024.
ISSN: ESSN 1439-7633
PubMed: 38642076
DOI: 10.1002/CBIC.202400235