Zinc in PDB 8hpi: Crystal Structure of Tyrosinase From Priestia Megaterium

The structure of Crystal Structure of Tyrosinase From Priestia Megaterium, PDB code: 8hpi was solved by Y.Huang, W.Song, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.98 / 2.54
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	104.95, 104.95, 137.98, 90, 90, 90
R / Rfree (%)	20 / 24.9

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 15;

Binding sites:

The binding sites of Zinc atom in the Crystal Structure of Tyrosinase From Priestia Megaterium (pdb code 8hpi). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 15 binding sites of Zinc where determined in the Crystal Structure of Tyrosinase From Priestia Megaterium, PDB code: 8hpi:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 15 in the Crystal Structure of Tyrosinase From Priestia Megaterium


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 Tyrosinase From Priestia Megaterium within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:65.8 occ:1.00 O A:HOH472 2.1 49.8 1.0 O A:HOH461 2.1 49.5 1.0 OD2 A:ASP287 2.1 45.4 1.0 ND1 A:HIS13 2.3 53.7 1.0 CG A:ASP287 3.1 39.0 1.0 CG A:HIS13 3.3 50.5 1.0 CE1 A:HIS13 3.3 53.8 1.0 CB A:HIS13 3.5 47.1 1.0 CB A:ASP287 3.6 39.1 1.0 OD1 A:ASP287 4.2 36.9 1.0 CD2 A:HIS13 4.4 48.9 1.0 NE2 A:HIS13 4.4 49.6 1.0 N A:ASN10 4.7 34.8 1.0 CB A:LYS9 4.8 38.8 1.0 CG A:LYS9 4.9 41.1 1.0 CB A:ASN10 5.0 35.7 1.0

Zinc binding site 2 out of 15 in the Crystal Structure of Tyrosinase From Priestia Megaterium


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 Tyrosinase From Priestia Megaterium within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:30.5 occ:1.00 NE2 A:HIS60 2.0 29.0 1.0 O A:HOH410 2.0 29.7 1.0 O A:HOH465 2.1 24.9 1.0 NE2 A:HIS42 2.1 31.6 1.0 O A:HOH469 2.5 20.6 1.0 CE1 A:HIS60 2.9 29.6 1.0 CD2 A:HIS60 3.0 27.8 1.0 CE1 A:HIS42 3.0 33.1 1.0 CD2 A:HIS42 3.2 30.2 1.0 ZN A:ZN303 3.5 28.8 1.0 NE2 A:HIS69 3.8 23.7 1.0 O A:HOH476 3.9 28.2 1.0 CE2 A:PHE227 4.0 25.4 1.0 ND1 A:HIS60 4.0 29.2 1.0 CG A:HIS60 4.1 29.1 1.0 ND1 A:HIS42 4.2 29.7 1.0 CZ A:PHE227 4.3 25.4 1.0 CG A:HIS42 4.3 29.0 1.0 CE1 A:HIS69 4.3 22.5 1.0 NE2 A:HIS208 4.4 28.6 1.0 CE1 A:HIS208 4.6 28.9 1.0 NE2 A:HIS231 4.7 28.7 1.0 CG1 A:VAL218 4.8 33.6 1.0 CG2 A:VAL218 4.9 34.0 1.0 NE2 A:HIS204 4.9 28.2 1.0

Zinc binding site 3 out of 15 in the Crystal Structure of Tyrosinase From Priestia Megaterium


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 Tyrosinase From Priestia Megaterium within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn303 b:28.8 occ:1.00 O A:HOH410 2.0 29.7 1.0 NE2 A:HIS231 2.0 28.7 1.0 NE2 A:HIS208 2.1 28.6 1.0 NE2 A:HIS204 2.1 28.2 1.0 CE1 A:HIS231 3.0 28.8 1.0 CD2 A:HIS208 3.0 28.8 1.0 CD2 A:HIS204 3.0 28.2 1.0 CD2 A:HIS231 3.0 29.2 1.0 CE1 A:HIS208 3.1 28.9 1.0 O A:HOH469 3.1 20.6 1.0 CE1 A:HIS204 3.1 28.1 1.0 ZN A:ZN302 3.5 30.5 1.0 CE2 A:PHE227 3.9 25.4 1.0 NE2 A:HIS69 4.1 23.7 1.0 O A:HOH465 4.1 24.9 1.0 ND1 A:HIS231 4.1 28.1 1.0 ND1 A:HIS208 4.2 28.2 1.0 CG A:HIS208 4.2 29.0 1.0 CG A:HIS231 4.2 28.0 1.0 ND1 A:HIS204 4.2 27.7 1.0 CG A:HIS204 4.2 28.1 1.0 CZ A:PHE227 4.2 25.4 1.0 CD2 A:HIS230 4.5 26.3 1.0 O A:HOH476 4.5 28.2 1.0 NE2 A:HIS230 4.6 26.0 1.0 CD2 A:HIS69 4.6 23.3 1.0 CE1 A:PHE65 4.6 30.7 1.0 CD2 A:PHE227 4.7 25.8 1.0 NE2 A:HIS60 4.7 29.0 1.0 CE1 A:HIS69 4.8 22.5 1.0 CD2 A:HIS60 4.9 27.8 1.0

Zinc binding site 4 out of 15 in the Crystal Structure of Tyrosinase From Priestia Megaterium


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 Tyrosinase From Priestia Megaterium within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn304 b:74.0 occ:1.00 O B:HOH407 2.0 76.2 1.0 NE2 A:HIS49 2.2 34.9 1.0 O B:HOH436 2.6 57.0 1.0 O B:HOH470 2.8 27.6 1.0 OD1 B:ASN144 2.9 38.0 1.0 CE1 A:HIS49 3.1 35.4 1.0 CD2 A:HIS49 3.3 32.6 1.0 CG B:ASN144 3.7 38.0 1.0 ND2 B:ASN144 3.8 37.1 1.0 ND1 A:HIS49 4.2 33.0 1.0 O B:GLN142 4.2 42.8 1.0 CG A:HIS49 4.3 32.6 1.0 CA A:LYS47 4.6 34.1 1.0 O A:LYS47 4.6 32.3 1.0 CG A:LYS47 4.8 45.5 1.0 CB A:LYS47 5.0 39.6 1.0

Zinc binding site 5 out of 15 in the Crystal Structure of Tyrosinase From Priestia Megaterium


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 Tyrosinase From Priestia Megaterium within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn305 b:89.9 occ:1.00 OD1 A:ASP275 2.4 38.7 1.0 O A:HOH427 2.8 37.6 1.0 CG A:ASP275 3.1 33.5 1.0 OD2 A:ASP275 3.2 32.0 1.0 OG1 A:THR272 3.7 27.0 1.0 CG2 A:THR272 4.3 24.7 1.0 OE2 A:GLU274 4.4 33.4 1.0 CB A:ASP275 4.4 31.6 1.0 CB A:THR272 4.6 25.4 1.0 N A:ASP275 4.8 30.7 1.0 CA A:ASP275 4.8 30.7 1.0

Zinc binding site 6 out of 15 in the Crystal Structure of Tyrosinase From Priestia Megaterium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of Tyrosinase From Priestia Megaterium within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn306 b:84.2 occ:1.00 O A:HOH409 2.1 64.1 1.0 O A:HOH453 2.1 77.3 1.0 O A:HOH475 2.1 75.9 1.0 O A:HOH477 2.1 65.8 1.0 ND1 A:HIS245 2.3 55.4 1.0 CE1 A:HIS245 3.2 51.6 1.0 CG A:HIS245 3.4 46.9 1.0 CB A:HIS245 3.8 41.5 1.0 CA A:HIS245 4.1 39.9 1.0 OD1 A:ASP247 4.2 52.4 1.0 O A:VAL244 4.3 41.9 1.0 NE2 A:HIS245 4.3 48.3 1.0 CD2 A:HIS245 4.4 47.2 1.0 CG2 A:THR175 4.6 43.2 1.0 CA A:THR175 4.7 41.1 1.0 O A:THR175 4.7 39.9 1.0 CB A:THR175 4.9 42.1 1.0 OD2 A:ASP247 4.9 53.3 1.0 CG A:ASP247 4.9 53.0 1.0 N A:HIS245 4.9 39.4 1.0

Zinc binding site 7 out of 15 in the Crystal Structure of Tyrosinase From Priestia Megaterium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Crystal Structure of Tyrosinase From Priestia Megaterium within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn307 b:119.8 occ:1.00 O A:HOH404 2.1 22.1 1.0 OD1 A:ASP123 2.5 64.2 1.0 OD2 A:ASP123 2.7 60.2 1.0 CG A:ASP123 2.9 54.9 1.0 O A:HOH470 3.1 61.1 1.0 O1 A:EDO310 4.2 61.3 1.0 CB A:ASP123 4.5 49.1 1.0 NZ A:LYS150 4.8 42.3 1.0

Zinc binding site 8 out of 15 in the Crystal Structure of Tyrosinase From Priestia Megaterium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Crystal Structure of Tyrosinase From Priestia Megaterium within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:104.6 occ:1.00 OD2 B:ASP287 2.2 36.9 1.0 ND1 B:HIS13 2.4 31.8 1.0 CG B:ASP287 3.1 38.8 1.0 CG B:HIS13 3.2 30.9 1.0 CE1 B:HIS13 3.4 32.6 1.0 CB B:HIS13 3.4 32.1 1.0 CB B:ASP287 3.5 39.4 1.0 OD1 B:ASP287 4.2 39.0 1.0 CD2 B:HIS13 4.4 30.9 1.0 NE2 B:HIS13 4.4 31.9 1.0 CA B:ASP287 4.8 41.2 1.0 CB B:LYS9 4.8 38.9 1.0 CG B:LYS9 4.9 41.4 1.0 CA B:HIS13 4.9 33.8 1.0 N B:ASN10 4.9 34.5 1.0

Zinc binding site 9 out of 15 in the Crystal Structure of Tyrosinase From Priestia Megaterium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Crystal Structure of Tyrosinase From Priestia Megaterium within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:80.4 occ:1.00 NE2 B:HIS13 2.4 31.9 1.0 CE1 B:HIS13 2.9 32.6 1.0 CD2 B:HIS13 3.6 30.9 1.0 ND1 B:HIS13 4.1 31.8 1.0 CG B:HIS13 4.4 30.9 1.0

Zinc binding site 10 out of 15 in the Crystal Structure of Tyrosinase From Priestia Megaterium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Crystal Structure of Tyrosinase From Priestia Megaterium within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn303 b:26.0 occ:1.00 NE2 B:HIS60 2.0 24.6 1.0 O B:HOH403 2.0 23.6 1.0 O B:HOH458 2.0 22.5 1.0 NE2 B:HIS42 2.1 23.9 1.0 O B:HOH452 2.6 17.5 1.0 CE1 B:HIS60 2.9 25.6 1.0 CE1 B:HIS42 3.0 25.5 1.0 CD2 B:HIS60 3.0 24.0 1.0 CD2 B:HIS42 3.2 23.0 1.0 ZN B:ZN304 3.4 24.3 1.0 NE2 B:HIS69 3.8 24.0 1.0 CE2 B:PHE227 4.0 23.6 1.0 ND1 B:HIS60 4.1 25.3 1.0 O B:HOH467 4.1 18.3 1.0 CG B:HIS60 4.1 25.3 1.0 ND1 B:HIS42 4.1 24.6 1.0 CG B:HIS42 4.2 23.4 1.0 CZ B:PHE227 4.3 23.4 1.0 CE1 B:HIS69 4.3 23.5 1.0 NE2 B:HIS208 4.4 23.7 1.0 CE1 B:HIS208 4.6 24.1 1.0 CG2 B:VAL218 4.7 31.0 1.0 NE2 B:HIS231 4.8 24.1 1.0 CG1 B:VAL218 4.8 30.9 1.0 NE2 B:HIS204 4.9 25.4 1.0 CA B:VAL218 4.9 30.1 1.0

Y.Huang, W.Song. Crystal Structure of Tyrosinase From Priestia Megaterium To Be Published.