Zinc in PDB 1cg2: Carboxypeptidase G2

All present enzymatic activity of Carboxypeptidase G2:
3.4.17.11;

The structure of Carboxypeptidase G2, PDB code: 1cg2 was solved by S.Rowsell, R.A.Pauptit, A.D.Tucker, R.G.Melton, D.M.Blow, P.Brick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	81.260, 105.280, 122.190, 90.00, 109.54, 90.00
R / Rfree (%)	19.6 / 22.4

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 13;

Binding sites:

The binding sites of Zinc atom in the Carboxypeptidase G2 (pdb code 1cg2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 13 binding sites of Zinc where determined in the Carboxypeptidase G2, PDB code: 1cg2:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 13 in the Carboxypeptidase G2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Carboxypeptidase G2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:22.1 occ:1.00 O A:HOH538 1.9 7.3 1.0 NE2 A:HIS385 2.0 28.7 1.0 OD2 A:ASP141 2.0 22.6 1.0 OE2 A:GLU176 2.1 27.3 1.0 OE1 A:GLU176 2.5 28.3 1.0 CD A:GLU176 2.6 27.8 1.0 CE1 A:HIS385 2.9 28.6 1.0 CG A:ASP141 2.9 18.5 1.0 CD2 A:HIS385 3.0 30.1 1.0 OD1 A:ASP141 3.1 11.6 1.0 ZN A:ZN501 3.2 19.4 1.0 O A:HOH509 3.9 15.9 1.0 O A:HOH556 4.0 36.9 1.0 ND1 A:HIS385 4.0 29.0 1.0 OE1 A:GLU175 4.1 14.5 1.0 CG A:GLU176 4.1 26.8 1.0 CG A:HIS385 4.1 29.1 1.0 CB A:ASP141 4.3 19.1 1.0 CG1 A:VAL116 4.3 23.8 1.0 NE2 A:HIS112 4.4 12.1 1.0 CE1 A:HIS112 4.4 11.8 1.0 O A:HOH523 4.6 31.9 1.0 OE1 A:GLU200 4.8 21.9 1.0

Zinc binding site 2 out of 13 in the Carboxypeptidase G2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Carboxypeptidase G2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:19.4 occ:1.00 OD1 A:ASP141 2.0 11.6 1.0 OE1 A:GLU200 2.0 21.9 1.0 NE2 A:HIS112 2.1 12.1 1.0 O A:HOH538 2.2 7.3 1.0 OE2 A:GLU200 2.5 19.1 1.0 CD A:GLU200 2.5 20.2 1.0 CE1 A:HIS112 3.0 11.8 1.0 CG A:ASP141 3.0 18.5 1.0 CD2 A:HIS112 3.1 13.5 1.0 ZN A:ZN500 3.2 22.1 1.0 OD2 A:ASP141 3.5 22.6 1.0 OE1 A:GLU175 3.5 14.5 1.0 O A:HOH556 4.0 36.9 1.0 OE2 A:GLU176 4.0 27.3 1.0 CG A:GLU200 4.0 21.3 1.0 CB A:ASP142 4.1 19.9 1.0 CD A:GLU175 4.1 16.8 1.0 ND1 A:HIS112 4.1 13.4 1.0 CG A:HIS112 4.2 14.3 1.0 CB A:ASP141 4.4 19.1 1.0 CD A:GLU176 4.4 27.8 1.0 OE1 A:GLU176 4.5 28.3 1.0 CG A:ASP142 4.6 20.4 1.0 OE2 A:GLU175 4.6 16.9 1.0 O A:HOH523 4.7 31.9 1.0 CD A:PRO201 4.7 23.8 1.0 CB A:GLU200 4.7 22.5 1.0 CA A:ASP141 4.7 21.2 1.0 C A:ASP141 4.9 20.7 1.0 CG A:GLU175 4.9 18.0 1.0 OD2 A:ASP142 4.9 19.2 1.0 N A:ASP142 5.0 20.5 1.0

Zinc binding site 3 out of 13 in the Carboxypeptidase G2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Carboxypeptidase G2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:43.5 occ:1.00 OD2 C:ASP387 1.9 38.7 1.0 O C:HOH503 1.9 25.1 1.0 ND1 A:HIS229 2.0 27.8 1.0 O A:HOH521 2.3 14.2 1.0 CG A:HIS229 2.9 29.1 1.0 CG C:ASP387 2.9 37.0 1.0 CE1 A:HIS229 3.1 28.7 1.0 CB A:HIS229 3.2 30.4 1.0 OD1 C:ASP387 3.3 36.6 1.0 ND2 A:ASN275 4.1 34.8 1.0 CD2 A:HIS229 4.1 28.7 1.0 NE2 A:HIS229 4.1 29.4 1.0 CB C:ASP387 4.2 35.8 1.0 CA A:HIS229 4.4 31.6 1.0 N A:GLY231 4.7 35.2 1.0 CA A:GLY231 4.8 35.1 1.0

Zinc binding site 4 out of 13 in the Carboxypeptidase G2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Carboxypeptidase G2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn503 b:28.2 occ:1.00 O A:HOH564 2.1 2.0 1.0 O A:HOH563 2.2 16.9 1.0 OD2 A:ASP256 2.3 38.5 1.0 OD1 A:ASP256 2.5 36.8 1.0 CG A:ASP256 2.7 36.0 1.0 CB A:ASP256 4.2 34.5 1.0 CB A:ALA258 4.3 35.5 1.0 CG A:LYS259 4.9 37.4 1.0

Zinc binding site 5 out of 13 in the Carboxypeptidase G2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Carboxypeptidase G2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn500 b:24.7 occ:1.00 O B:HOH580 1.9 18.9 1.0 NE2 B:HIS385 2.0 30.6 1.0 OD2 B:ASP141 2.0 26.0 1.0 OE2 B:GLU176 2.1 28.7 1.0 OE1 B:GLU176 2.5 29.5 1.0 CD B:GLU176 2.6 28.7 1.0 CG B:ASP141 2.8 24.0 1.0 CE1 B:HIS385 2.9 31.0 1.0 OD1 B:ASP141 3.0 18.9 1.0 CD2 B:HIS385 3.0 30.8 1.0 ZN B:ZN501 3.2 21.1 1.0 O B:HOH508 3.8 16.9 1.0 ND1 B:HIS385 4.0 30.1 1.0 OE1 B:GLU175 4.1 19.8 1.0 CG B:HIS385 4.1 29.9 1.0 CG B:GLU176 4.1 28.8 1.0 O B:HOH559 4.3 43.4 1.0 CB B:ASP141 4.3 24.1 1.0 CG1 B:VAL116 4.3 23.3 1.0 NE2 B:HIS112 4.4 11.6 1.0 CE1 B:HIS112 4.4 12.1 1.0 O B:HOH526 4.5 34.2 1.0 OE1 B:GLU200 4.7 19.5 1.0

Zinc binding site 6 out of 13 in the Carboxypeptidase G2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Carboxypeptidase G2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:21.1 occ:1.00 OD1 B:ASP141 1.9 18.9 1.0 OE1 B:GLU200 2.0 19.5 1.0 NE2 B:HIS112 2.1 11.6 1.0 O B:HOH580 2.1 18.9 1.0 OE2 B:GLU200 2.5 19.5 1.0 CD B:GLU200 2.6 20.4 1.0 CE1 B:HIS112 3.0 12.1 1.0 CG B:ASP141 3.1 24.0 1.0 CD2 B:HIS112 3.1 13.1 1.0 ZN B:ZN500 3.2 24.7 1.0 OE1 B:GLU175 3.5 19.8 1.0 OD2 B:ASP141 3.6 26.0 1.0 OE2 B:GLU176 4.0 28.7 1.0 CB B:ASP142 4.1 24.3 1.0 CG B:GLU200 4.1 21.0 1.0 ND1 B:HIS112 4.1 13.8 1.0 CD B:GLU175 4.2 19.4 1.0 CG B:HIS112 4.2 14.1 1.0 O B:HOH559 4.3 43.4 1.0 CB B:ASP141 4.3 24.1 1.0 CD B:GLU176 4.4 28.7 1.0 OE1 B:GLU176 4.4 29.5 1.0 O B:HOH526 4.5 34.2 1.0 CG B:ASP142 4.6 25.2 1.0 OE2 B:GLU175 4.6 19.1 1.0 CA B:ASP141 4.7 25.0 1.0 CD B:PRO201 4.7 21.9 1.0 CB B:GLU200 4.8 22.0 1.0 C B:ASP141 4.8 24.7 1.0 OD2 B:ASP142 5.0 24.4 1.0 N B:ASP142 5.0 24.3 1.0 CG B:GLU175 5.0 21.2 1.0 NE2 B:HIS385 5.0 30.6 1.0

Zinc binding site 7 out of 13 in the Carboxypeptidase G2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Carboxypeptidase G2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:43.4 occ:1.00 ND1 B:HIS229 2.0 29.4 1.0 OD2 D:ASP387 2.0 39.2 1.0 O B:HOH525 2.3 34.5 1.0 O B:HOH523 2.4 10.8 1.0 CE1 B:HIS229 2.9 30.2 1.0 CG B:HIS229 3.0 30.5 1.0 CG D:ASP387 3.1 38.4 1.0 CB B:HIS229 3.3 32.0 1.0 OD1 D:ASP387 3.5 38.6 1.0 ND2 B:ASN275 4.0 33.2 1.0 NE2 B:HIS229 4.0 30.9 1.0 CD2 B:HIS229 4.1 30.3 1.0 CB D:ASP387 4.4 38.1 1.0 CA B:HIS229 4.6 33.2 1.0 N B:GLY231 4.9 35.7 1.0

Zinc binding site 8 out of 13 in the Carboxypeptidase G2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Carboxypeptidase G2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn500 b:28.8 occ:1.00 NE2 C:HIS385 1.9 31.7 1.0 O C:HOH539 1.9 23.6 1.0 OD2 C:ASP141 2.1 30.2 1.0 OE2 C:GLU176 2.1 29.1 1.0 OE1 C:GLU176 2.5 28.5 1.0 CD C:GLU176 2.6 29.2 1.0 CE1 C:HIS385 2.8 32.0 1.0 CD2 C:HIS385 3.0 31.9 1.0 CG C:ASP141 3.0 28.5 1.0 OD1 C:ASP141 3.3 27.1 1.0 ZN C:ZN501 3.3 28.6 1.0 O C:HOH510 3.7 24.3 1.0 O C:HOH555 3.9 44.6 1.0 ND1 C:HIS385 3.9 31.9 1.0 CG C:HIS385 4.0 31.6 1.0 OE1 C:GLU175 4.1 23.0 1.0 CG C:GLU176 4.1 29.3 1.0 CG1 C:VAL116 4.3 27.1 1.0 CB C:ASP141 4.3 28.9 1.0 O C:HOH526 4.5 34.5 1.0 NE2 C:HIS112 4.5 16.1 1.0 CE1 C:HIS112 4.5 19.2 1.0 OE1 C:GLU200 4.8 28.3 1.0

Zinc binding site 9 out of 13 in the Carboxypeptidase G2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Carboxypeptidase G2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn501 b:28.6 occ:1.00 OD1 C:ASP141 2.0 27.1 1.0 OE1 C:GLU200 2.0 28.3 1.0 NE2 C:HIS112 2.0 16.1 1.0 O C:HOH539 2.3 23.6 1.0 OE2 C:GLU200 2.5 27.4 1.0 CD C:GLU200 2.6 28.4 1.0 CG C:ASP141 2.9 28.5 1.0 CE1 C:HIS112 3.0 19.2 1.0 CD2 C:HIS112 3.1 19.5 1.0 OD2 C:ASP141 3.3 30.2 1.0 ZN C:ZN500 3.3 28.8 1.0 OE1 C:GLU175 3.5 23.0 1.0 OE2 C:GLU176 3.9 29.1 1.0 O C:HOH555 3.9 44.6 1.0 CB C:ASP142 4.0 28.1 1.0 CG C:GLU200 4.1 27.9 1.0 ND1 C:HIS112 4.1 20.1 1.0 CG C:HIS112 4.2 20.7 1.0 CD C:GLU175 4.2 23.4 1.0 CB C:ASP141 4.3 28.9 1.0 CD C:GLU176 4.4 29.2 1.0 O C:HOH526 4.5 34.5 1.0 OE1 C:GLU176 4.5 28.5 1.0 CG C:ASP142 4.5 27.9 1.0 CA C:ASP141 4.6 29.2 1.0 CD C:PRO201 4.7 26.7 1.0 OE2 C:GLU175 4.7 22.8 1.0 CB C:GLU200 4.7 27.5 1.0 C C:ASP141 4.8 29.0 1.0 N C:ASP142 4.9 28.9 1.0 OD2 C:ASP142 4.9 26.2 1.0 CA C:ASP142 4.9 28.9 1.0 OD1 C:ASP142 5.0 28.1 1.0 CG C:GLU175 5.0 23.8 1.0 NE2 C:HIS385 5.0 31.7 1.0

Zinc binding site 10 out of 13 in the Carboxypeptidase G2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Carboxypeptidase G2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn502 b:37.0 occ:1.00 OD2 A:ASP387 1.9 35.7 1.0 ND1 C:HIS229 2.1 27.0 1.0 O C:HOH524 2.3 5.0 1.0 O A:HOH593 2.4 31.6 1.0 CG A:ASP387 3.0 33.8 1.0 CE1 C:HIS229 3.1 27.3 1.0 CG C:HIS229 3.1 28.0 1.0 OD1 A:ASP387 3.4 33.9 1.0 CB C:HIS229 3.4 29.8 1.0 ND2 C:ASN275 3.9 34.5 1.0 NE2 C:HIS229 4.2 27.7 1.0 CD2 C:HIS229 4.2 27.7 1.0 CB A:ASP387 4.2 32.8 1.0 CA C:HIS229 4.7 30.8 1.0 N C:GLY231 4.9 33.7 1.0

S.Rowsell, R.A.Pauptit, A.D.Tucker, R.G.Melton, D.M.Blow, P.Brick. Crystal Structure of Carboxypeptidase G2, A Bacterial Enzyme with Applications in Cancer Therapy. Structure V. 5 337 1997.
ISSN: ISSN 0969-2126
PubMed: 9083113
DOI: 10.1016/S0969-2126(97)00191-3