Zinc in PDB 3hpi: Crystal Structure of Maltose-Binding Protein Mutant with Bound Sucrose

The structure of Crystal Structure of Maltose-Binding Protein Mutant with Bound Sucrose, PDB code: 3hpi was solved by A.D.Gould, B.H.Shilton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.80 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.042, 85.229, 132.864, 90.00, 90.00, 90.00
R / Rfree (%)	22.8 / 28.4

The binding sites of Zinc atom in the Crystal Structure of Maltose-Binding Protein Mutant with Bound Sucrose (pdb code 3hpi). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Crystal Structure of Maltose-Binding Protein Mutant with Bound Sucrose, PDB code: 3hpi:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in the Crystal Structure of Maltose-Binding Protein Mutant with Bound Sucrose


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 Maltose-Binding Protein Mutant with Bound Sucrose within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn372 b:37.8 occ:1.00 NE2 A:HIS203 2.1 28.4 1.0 O A:ACT375 2.5 42.9 1.0 O A:HOH373 2.5 42.7 1.0 OXT A:ACT375 2.6 41.4 1.0 C A:ACT375 2.9 43.0 1.0 CE1 A:HIS203 3.0 28.1 1.0 CD2 A:HIS203 3.1 28.6 1.0 ND1 A:HIS203 4.2 25.5 1.0 CG A:HIS203 4.2 28.6 1.0 CB A:PRO133 4.2 30.4 1.0 CB A:ASN201 4.3 36.7 1.0 CH3 A:ACT375 4.4 44.2 1.0 OD1 A:ASN201 4.6 36.5 1.0 CG A:ASN201 4.8 37.2 1.0 O A:ASN201 4.9 34.7 1.0 CA A:PRO133 4.9 30.3 1.0 O A:PRO133 5.0 30.6 1.0

Zinc binding site 2 out of 6 in the Crystal Structure of Maltose-Binding Protein Mutant with Bound Sucrose


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 Maltose-Binding Protein Mutant with Bound Sucrose within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn374 b:60.6 occ:1.00 OD2 A:ASP209 2.2 34.2 1.0 OE1 B:GLU38 2.5 34.9 1.0 OE2 B:GLU38 2.9 36.2 1.0 CD B:GLU38 3.1 32.6 1.0 CG A:ASP209 3.1 30.5 1.0 CB A:ASP209 3.3 26.0 1.0 O A:ASP207 4.0 27.1 1.0 OD1 A:ASP209 4.2 30.4 1.0 CG B:GLU38 4.6 30.8 1.0 CA A:ASP209 4.7 25.7 1.0 CG A:GLN152 4.8 27.2 1.0 N A:ASP209 4.9 25.3 1.0 O A:HOH377 4.9 27.0 1.0

Zinc binding site 3 out of 6 in the Crystal Structure of Maltose-Binding Protein Mutant with Bound Sucrose


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 Maltose-Binding Protein Mutant with Bound Sucrose within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn373 b:78.1 occ:1.00 O B:HOH426 2.5 28.2 1.0 CB B:SER211 2.8 22.5 1.0 NE2 A:HIS39 3.3 35.9 1.0 OD2 B:ASP209 3.4 27.2 1.0 N B:SER211 3.5 23.6 1.0 O A:HOH456 3.5 41.1 1.0 OG B:SER211 3.5 28.9 1.0 CG B:ASP209 3.7 26.5 1.0 CA B:SER211 3.7 24.3 1.0 OD1 B:ASP209 3.8 28.1 1.0 CE1 A:HIS39 4.0 37.1 1.0 CD2 A:HIS39 4.0 36.7 1.0 O A:HOH433 4.5 28.8 1.0 CB B:ASP209 4.6 22.8 1.0 C B:TYR210 4.7 23.5 1.0 N B:TYR210 4.7 21.8 1.0 ND1 A:HIS39 4.9 35.4 1.0 CB B:TYR210 4.9 22.7 1.0 C B:SER211 4.9 24.1 1.0 CG A:HIS39 4.9 36.2 1.0 N B:ILE212 4.9 25.7 1.0

Zinc binding site 4 out of 6 in the Crystal Structure of Maltose-Binding Protein Mutant with Bound Sucrose


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 Maltose-Binding Protein Mutant with Bound Sucrose within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn374 b:80.7 occ:1.00 OE2 A:GLU38 2.5 46.6 1.0 OD2 B:ASP209 2.5 27.2 1.0 CD A:GLU38 3.2 43.5 1.0 CG B:ASP209 3.3 26.5 1.0 CB B:ASP209 3.4 22.8 1.0 CG A:GLU38 3.6 41.2 1.0 O B:ASP207 4.0 28.9 1.0 OE1 A:GLU38 4.1 47.4 1.0 OD1 B:ASP209 4.4 28.1 1.0 O B:HOH426 4.4 28.2 1.0 CG B:GLN152 4.5 25.7 1.0 CA B:ASP209 4.7 23.1 1.0 CB A:GLU38 4.7 34.6 1.0 CD B:GLN152 4.8 28.2 1.0 N B:ASP209 4.9 23.2 1.0

Zinc binding site 5 out of 6 in the Crystal Structure of Maltose-Binding Protein Mutant with Bound Sucrose


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 Maltose-Binding Protein Mutant with Bound Sucrose within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn371 b:37.4 occ:1.00 NE2 B:HIS39 2.3 28.2 1.0 OG A:SER211 2.3 16.3 1.0 O A:HOH377 2.6 27.0 1.0 O A:HOH376 2.6 34.0 1.0 O A:HOH409 2.7 46.1 1.0 CB A:SER211 3.1 20.7 1.0 CE1 B:HIS39 3.2 28.2 1.0 CD2 B:HIS39 3.3 27.0 1.0 N A:SER211 4.0 24.8 1.0 OD2 A:ASP209 4.1 34.2 1.0 CA A:SER211 4.1 23.7 1.0 ND1 B:HIS39 4.3 26.2 1.0 CG A:ASP209 4.3 30.5 1.0 CG B:HIS39 4.4 25.4 1.0 OD1 A:ASP209 4.4 30.4 1.0 O B:HOH440 4.4 30.2 1.0 OH B:TYR17 4.9 31.7 1.0 CE1 B:TYR17 4.9 30.8 1.0

Zinc binding site 6 out of 6 in the Crystal Structure of Maltose-Binding Protein Mutant with Bound Sucrose


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 Maltose-Binding Protein Mutant with Bound Sucrose within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn372 b:36.6 occ:1.00 NE2 B:HIS203 2.1 23.7 1.0 O B:HOH377 2.2 27.5 1.0 O B:ACT376 2.4 44.8 1.0 CD2 B:HIS203 3.1 23.2 1.0 CE1 B:HIS203 3.1 24.1 1.0 OXT B:ACT376 3.2 48.2 1.0 C B:ACT376 3.2 46.6 1.0 CB B:PRO133 4.0 25.5 1.0 ND1 B:HIS203 4.2 25.3 1.0 CG B:HIS203 4.3 26.6 1.0 OD1 B:ASN201 4.4 37.9 1.0 CB B:ASN201 4.4 35.7 1.0 CH3 B:ACT376 4.7 46.6 1.0 CG B:ASN201 4.7 35.6 1.0 CA B:PRO133 4.8 23.6 1.0 O B:PRO133 4.8 23.5 1.0 C B:PRO133 4.9 25.3 1.0

A.D.Gould, B.H.Shilton. Studies of the Maltose Transport System Reveal A Mechanism For Coupling Atp Hydrolysis to Substrate Translocation Without Direct Recognition of Substrate. J.Biol.Chem. V. 285 11290 2010.
ISSN: ISSN 0021-9258
PubMed: 20147285
DOI: 10.1074/JBC.M109.089078