Zinc in PDB 6xj5: Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design

All present enzymatic activity of Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design:
3.4.17.11;

The structure of Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design, PDB code: 6xj5 was solved by B.J.Yachnin, W.A.Hansen, S.D.Khare, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.50 / 3.11
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	72.12, 188.46, 124.5, 90, 90.17, 90
R / Rfree (%)	27.1 / 30.9

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 40; Page 5, Binding sites: 41 - 50; Page 6, Binding sites: 51 - 56;

Binding sites:

The binding sites of Zinc atom in the Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design (pdb code 6xj5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 56 binding sites of Zinc where determined in the Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design, PDB code: 6xj5:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 56 in the Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:55.5 occ:1.00 NE2 A:HIS385 2.0 54.7 1.0 O A:HOH708 2.0 42.9 1.0 OD2 A:ASP141 2.1 56.8 1.0 OE2 A:GLU176 2.1 58.2 1.0 OE1 A:GLU176 2.5 57.5 1.0 CD A:GLU176 2.6 59.4 1.0 CG A:ASP141 2.8 58.2 1.0 CE1 A:HIS385 2.9 54.6 1.0 CD2 A:HIS385 3.0 54.5 1.0 OD1 A:ASP141 3.1 57.4 1.0 ZN A:ZN501 3.2 56.0 1.0 OE1 A:GLU175 3.7 64.8 1.0 CB A:ASP141 4.0 58.8 1.0 ND1 A:HIS385 4.0 54.4 1.0 CG A:GLU176 4.0 60.1 1.0 CG A:HIS385 4.1 54.2 1.0 O A:HOH716 4.1 28.7 1.0 NE2 A:HIS112 4.3 56.2 1.0 CE1 A:HIS112 4.3 56.2 1.0 CG1 A:VAL116 4.5 61.4 1.0 OE2 A:GLU200 4.6 58.5 1.0 CD A:GLU175 4.7 63.6 1.0

Zinc binding site 2 out of 56 in the Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:56.0 occ:1.00 OD1 A:ASP141 2.0 57.4 1.0 NE2 A:HIS112 2.0 56.2 1.0 OE2 A:GLU200 2.1 58.5 1.0 OE1 A:GLU200 2.5 59.1 1.0 O A:HOH708 2.5 42.9 1.0 CD A:GLU200 2.6 60.2 1.0 CG A:ASP141 2.8 58.2 1.0 CE1 A:HIS112 3.0 56.2 1.0 CD2 A:HIS112 3.0 56.3 1.0 OD2 A:ASP141 3.0 56.8 1.0 ZN A:ZN500 3.2 55.5 1.0 OE1 A:GLU175 3.3 64.8 1.0 CD A:GLU175 3.9 63.6 1.0 CB A:ASP142 4.0 59.7 1.0 ND1 A:HIS112 4.1 56.5 1.0 CG A:GLU200 4.1 60.9 1.0 OE2 A:GLU176 4.1 58.2 1.0 CG A:HIS112 4.1 56.8 1.0 CB A:ASP141 4.2 58.8 1.0 CG A:ASP142 4.3 59.4 1.0 OE2 A:GLU175 4.3 62.2 1.0 O A:HOH716 4.4 28.7 1.0 CD A:PRO201 4.5 65.8 1.0 OD2 A:ASP142 4.5 59.2 1.0 CA A:ASP141 4.6 59.3 1.0 CD A:GLU176 4.6 59.4 1.0 CG A:GLU175 4.6 63.4 1.0 CB A:GLU200 4.7 62.1 1.0 OD1 A:ASP142 4.7 59.0 1.0 OE1 A:GLU176 4.8 57.5 1.0 CA A:ASP142 4.9 59.6 1.0 C A:ASP141 4.9 59.5 1.0

Zinc binding site 3 out of 56 in the Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:69.3 occ:1.00 ND1 A:HIS229 1.9 62.6 1.0 O A:HOH715 2.6 17.2 1.0 CE1 A:HIS229 2.7 62.8 1.0 CG A:HIS229 3.0 62.7 1.0 CB A:HIS229 3.5 63.3 1.0 NE2 A:HIS229 3.9 62.5 1.0 CD2 A:HIS229 4.0 62.5 1.0 ND2 A:ASN275 4.3 65.5 1.0 CA A:HIS229 4.7 63.8 1.0

Zinc binding site 4 out of 56 in the Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn602 b:88.0 occ:1.00 OD2 A:ASP59 1.8 79.6 1.0 CG A:ASP59 2.4 78.9 1.0 OD1 A:ASP59 2.4 79.5 1.0 O A:HOH701 2.5 66.2 1.0 CE A:LYS119 3.2 71.7 1.0 CG A:LYS119 3.5 70.9 1.0 CD A:LYS119 3.6 71.3 1.0 CB A:ASP59 3.9 78.1 1.0 O A:GLU54 3.9 70.4 1.0 OE1 A:GLU54 4.0 69.9 1.0 NZ A:LYS119 4.1 72.0 1.0 CB A:GLU54 4.2 70.0 1.0 N A:GLY62 4.3 70.2 1.0 CA A:GLY62 4.4 70.1 1.0 CB A:LYS119 4.7 70.3 1.0 CB A:GLU61 4.8 71.7 1.0 CA A:ASP59 4.9 77.2 1.0 C A:GLU54 4.9 69.8 1.0 CD A:GLU54 5.0 70.4 1.0

Zinc binding site 5 out of 56 in the Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn603 b:86.6 occ:1.00 OD2 A:ASP29 2.4 69.1 1.0 O A:HOH707 2.5 42.3 1.0 O A:HOH705 2.6 26.5 1.0 OD1 A:ASP29 2.9 68.7 1.0 CG A:ASP29 2.9 69.3 1.0 O A:HOH718 3.2 19.8 1.0 CG1 A:VAL31 3.8 67.2 1.0 CB A:VAL31 4.1 67.5 1.0 CB A:LEU32 4.1 65.7 1.0 N A:LEU32 4.2 66.5 1.0 CB A:ASP29 4.3 69.9 1.0 CA A:LEU32 4.6 65.7 1.0 C A:VAL31 4.8 67.5 1.0 CE A:MET409 4.9 69.1 1.0 O A:ASP29 5.0 71.0 1.0

Zinc binding site 6 out of 56 in the Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn604 b:111.5 occ:1.00 OE2 A:GLU71 2.0 72.5 1.0 OE2 E:GLU61 2.0 78.8 1.0 CD E:GLU61 2.7 77.9 1.0 CD A:GLU71 2.7 72.8 1.0 OE1 E:GLU61 2.9 78.0 1.0 OE1 A:GLU71 2.9 73.1 1.0 O A:HOH710 3.2 38.0 1.0 NE A:ARG83 3.8 73.8 1.0 CG E:GLU61 4.0 77.0 1.0 CG A:GLU71 4.1 72.4 1.0 NZ A:LYS75 4.4 75.0 1.0 CD A:ARG83 4.4 73.3 1.0 CZ A:ARG83 4.8 74.7 1.0 NH2 A:ARG83 4.8 74.5 1.0 CE A:LYS75 4.9 74.7 1.0

Zinc binding site 7 out of 56 in the Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn605 b:109.5 occ:1.00 OE1 A:GLU39 2.6 74.9 1.0 O A:HOH713 3.0 39.0 1.0 CD A:GLU39 3.5 74.0 1.0 OE2 A:GLU39 3.9 73.8 1.0 CG A:GLU39 4.8 73.2 1.0 CA A:GLU39 4.9 71.7 1.0

Zinc binding site 8 out of 56 in the Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn600 b:115.0 occ:1.00 N1 B:V44203 1.9 113.2 1.0 N3 B:V44203 1.9 114.4 1.0 SG A:CYS203 2.4 98.2 1.0 C5 B:V44203 2.8 113.2 1.0 C1 B:V44203 2.8 112.8 1.0 C2 B:V44203 3.0 112.7 1.0 O A:ALA204 3.0 84.7 1.0 C6 B:V44203 3.1 114.9 1.0 C9 B:V44203 3.3 111.1 1.0 N2 B:V44203 4.0 114.4 1.0 N4 B:V44203 4.0 114.3 1.0 CB A:CYS203 4.1 89.7 1.0 C3 B:V44203 4.1 113.6 1.0 C10 B:V44203 4.1 108.0 1.0 C7 B:V44203 4.1 115.0 1.0 C A:ALA204 4.2 84.0 1.0 N A:ALA204 4.3 83.9 1.0 C A:CYS203 4.4 84.2 1.0 CD1 A:PHE382 4.5 67.9 1.0 CA A:CYS203 4.7 85.9 1.0 O A:CYS203 4.8 82.7 1.0 CB A:ASP206 4.9 87.0 1.0 CE2 B:PHE382 4.9 66.2 1.0 CA A:ALA204 4.9 83.6 1.0 O A:GLY381 5.0 66.3 1.0

Zinc binding site 9 out of 56 in the Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn500 b:61.9 occ:1.00 NE2 B:HIS385 1.9 58.6 1.0 OD2 B:ASP141 2.1 61.9 1.0 OE2 B:GLU176 2.1 65.4 1.0 OE1 B:GLU176 2.5 64.8 1.0 CD B:GLU176 2.6 66.8 1.0 CG B:ASP141 2.8 62.5 1.0 CE1 B:HIS385 2.9 58.1 1.0 CD2 B:HIS385 2.9 58.0 1.0 OD1 B:ASP141 3.1 61.8 1.0 ZN B:ZN501 3.2 60.9 1.0 OE2 B:GLU175 3.7 72.2 1.0 CB B:ASP141 4.0 63.1 1.0 ND1 B:HIS385 4.0 57.5 1.0 CG B:GLU176 4.0 67.1 1.0 CG B:HIS385 4.1 57.1 1.0 CE1 B:HIS112 4.4 59.7 1.0 NE2 B:HIS112 4.4 59.4 1.0 CG1 B:VAL116 4.4 64.1 1.0 OE2 B:GLU200 4.6 63.3 1.0 CD B:GLU175 4.8 71.3 1.0

Zinc binding site 10 out of 56 in the Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Carboxypeptidase G2 Modified with A Versatile Bioconjugate For Metalloprotein Design within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:60.9 occ:1.00 OD1 B:ASP141 2.0 61.8 1.0 NE2 B:HIS112 2.1 59.4 1.0 OE2 B:GLU200 2.1 63.3 1.0 OE1 B:GLU200 2.5 63.7 1.0 CD B:GLU200 2.6 64.5 1.0 CG B:ASP141 2.8 62.5 1.0 OD2 B:ASP141 3.0 61.9 1.0 CE1 B:HIS112 3.0 59.7 1.0 CD2 B:HIS112 3.1 58.9 1.0 OE2 B:GLU175 3.2 72.2 1.0 ZN B:ZN500 3.2 61.9 1.0 CD B:GLU175 3.9 71.3 1.0 CB B:ASP142 4.0 68.0 1.0 CG B:GLU200 4.1 65.1 1.0 OE2 B:GLU176 4.1 65.4 1.0 ND1 B:HIS112 4.1 59.6 1.0 CB B:ASP141 4.2 63.1 1.0 CG B:HIS112 4.2 59.3 1.0 CG B:ASP142 4.3 69.2 1.0 OE1 B:GLU175 4.4 71.3 1.0 CD B:PRO201 4.4 74.4 1.0 OD2 B:ASP142 4.6 70.0 1.0 CD B:GLU176 4.6 66.8 1.0 CA B:ASP141 4.6 63.9 1.0 CG B:GLU175 4.6 70.7 1.0 CB B:GLU200 4.7 66.1 1.0 OD1 B:ASP142 4.8 70.7 1.0 OE1 B:GLU176 4.8 64.8 1.0 C B:ASP141 4.9 65.2 1.0 CA B:ASP142 5.0 67.0 1.0 NE2 B:HIS385 5.0 58.6 1.0

W.A.Hansen, B.J.Yachnin, W.A.Hansen, S.D.Khare. N/A N/A.