Zinc in PDB 2g2n: Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn

The structure of Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn, PDB code: 2g2n was solved by E.Lundberg, S.Backstrom, U.H.Sauer, A.E.Sauer-Eriksson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.05 / 1.65
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.970, 92.670, 58.050, 90.00, 103.86, 90.00
R / Rfree (%)	19.8 / 23.4

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 18;

Binding sites:

The binding sites of Zinc atom in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn (pdb code 2g2n). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 18 binding sites of Zinc where determined in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn, PDB code: 2g2n:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 18 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn


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 E.Coli Transthyretin-Related Protein with Bound Zn within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:37.0 occ:1.00 NE2 A:HIS98 2.0 21.4 1.0 ND1 A:HIS9 2.1 17.1 1.0 O A:HOH1026 2.2 24.4 1.0 O A:HOH1027 2.3 28.7 1.0 CE1 A:HIS98 2.8 22.1 1.0 CE1 A:HIS9 3.0 18.1 1.0 CD2 A:HIS98 3.1 20.5 1.0 CG A:HIS9 3.2 16.0 1.0 CB A:HIS9 3.5 15.1 1.0 ND1 A:HIS98 4.0 21.9 1.0 CG A:HIS98 4.2 19.2 1.0 NE2 A:HIS9 4.2 15.9 1.0 CD2 A:HIS9 4.3 16.3 1.0 N A:HIS9 4.4 15.2 1.0 C A:VAL8 4.5 15.4 1.0 O A:VAL8 4.6 15.4 1.0 CA A:HIS9 4.6 14.9 1.0 CG A:ARG47 4.6 16.5 1.0 ZN A:ZN1005 4.9 38.4 0.3 CD A:ARG47 5.0 19.0 1.0 CB A:SER7 5.0 14.6 1.0

Zinc binding site 2 out of 18 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn


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 E.Coli Transthyretin-Related Protein with Bound Zn within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1005 b:38.4 occ:0.30 CE1 A:HIS96 2.5 18.2 0.7 ND1 A:HIS98 2.6 21.9 1.0 CG A:HIS98 2.7 19.2 1.0 NE2 A:HIS96 2.7 17.9 0.3 O A:SER114 2.8 23.8 1.0 CB A:HIS98 3.1 17.4 1.0 CE1 A:HIS98 3.2 22.1 1.0 CD2 A:HIS98 3.2 20.5 1.0 ND1 A:HIS96 3.3 17.2 0.7 CD2 A:HIS96 3.3 17.3 0.3 NE2 A:HIS98 3.5 21.4 1.0 NE2 A:HIS96 3.6 16.7 0.7 CE1 A:HIS96 3.8 17.5 0.3 C A:SER114 3.9 23.4 1.0 ZN A:ZN1009 3.9 44.4 0.3 OXT A:SER114 4.2 24.9 1.0 CA A:HIS98 4.2 17.3 1.0 CB A:SER7 4.2 14.6 1.0 OG A:SER7 4.4 14.9 1.0 CG A:HIS96 4.5 17.1 0.7 CG A:HIS96 4.6 16.9 0.3 CD2 A:HIS96 4.7 17.3 0.7 ND1 A:HIS96 4.8 17.5 0.3 N A:HIS98 4.9 17.0 1.0 ZN A:ZN1001 4.9 37.0 1.0

Zinc binding site 3 out of 18 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn


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 E.Coli Transthyretin-Related Protein with Bound Zn within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1009 b:44.4 occ:0.35 OXT A:SER114 2.1 24.9 1.0 CD2 A:HIS96 2.2 17.3 0.3 ND1 A:HIS96 2.4 17.2 0.7 C A:SER114 3.0 23.4 1.0 CG A:HIS96 3.0 16.9 0.3 O A:SER114 3.2 23.8 1.0 CG A:HIS96 3.3 17.1 0.7 NE2 A:HIS96 3.3 17.9 0.3 CB A:HIS96 3.4 16.2 0.3 CE1 A:HIS96 3.4 18.2 0.7 CB A:HIS96 3.5 16.1 0.7 ZN A:ZN1005 3.9 38.4 0.3 O A:HIS96 4.1 15.9 0.3 ND1 A:HIS96 4.3 17.5 0.3 O A:HIS96 4.3 16.0 0.7 CE1 A:HIS96 4.4 17.5 0.3 CA A:SER114 4.4 22.9 1.0 C A:HIS96 4.5 15.8 0.3 CD2 A:HIS96 4.5 17.3 0.7 O A:HOH1025 4.5 32.8 1.0 NE2 A:HIS96 4.5 16.7 0.7 C A:HIS96 4.6 15.7 0.7 CA A:HIS96 4.6 16.2 0.3 CA A:HIS96 4.6 16.1 0.7 CB A:HIS98 4.9 17.4 1.0

Zinc binding site 4 out of 18 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn


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 E.Coli Transthyretin-Related Protein with Bound Zn within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1013 b:42.5 occ:0.55 OD1 A:ASP61 2.0 16.4 1.0 ND1 A:HIS89 2.0 17.1 1.0 O A:HOH1028 2.2 36.1 1.0 CE1 A:HIS89 2.8 16.6 1.0 CG A:HIS89 2.8 16.0 1.0 CG A:ASP61 3.0 15.8 1.0 CB A:HIS89 3.3 15.3 1.0 OD2 A:ASP61 3.3 17.0 1.0 NE2 A:HIS89 3.7 16.5 1.0 CD2 A:HIS89 3.8 17.6 1.0 CA A:HIS89 4.2 15.1 1.0 N A:ASP61 4.2 14.4 1.0 C A:GLY60 4.3 14.7 1.0 CB A:ASP61 4.3 14.2 1.0 CB B:PRO82 4.3 16.1 1.0 O A:HOH1075 4.4 42.8 1.0 CA A:ASP61 4.4 14.5 1.0 O A:GLY60 4.5 14.0 1.0 CA A:GLY60 4.7 15.5 1.0 CG B:PRO82 4.7 16.2 1.0 O A:HOH1074 4.9 39.5 1.0

Zinc binding site 5 out of 18 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn


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 E.Coli Transthyretin-Related Protein with Bound Zn within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1017 b:42.3 occ:0.50 OE2 A:GLU83 1.7 21.2 1.0 OE2 B:GLU87 2.1 16.0 1.0 O B:HOH1117 2.3 31.9 1.0 O A:HOH1030 2.4 35.3 1.0 CD A:GLU83 2.9 17.7 1.0 CD B:GLU87 3.0 15.5 1.0 O B:HOH1118 3.1 32.4 1.0 OE1 B:GLU87 3.2 13.7 1.0 CG A:GLU83 3.6 16.8 1.0 O B:HOH1169 3.7 42.9 1.0 OE1 A:GLU83 3.9 18.3 1.0 CZ2 B:TRP34 4.3 14.5 1.0 CG B:GLU87 4.3 16.6 1.0 CG1 A:VAL65 4.4 16.6 1.0 O A:HOH1032 4.5 31.5 1.0 CG A:PRO85 4.8 15.0 1.0 CG2 A:VAL65 4.8 17.3 1.0 NE1 B:TRP34 4.9 16.4 1.0 CE2 B:TRP34 4.9 14.7 1.0 CB A:PRO85 5.0 15.1 1.0

Zinc binding site 6 out of 18 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn


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 E.Coli Transthyretin-Related Protein with Bound Zn within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1002 b:31.5 occ:1.00 NE2 B:HIS98 1.9 18.6 1.0 ND1 B:HIS9 2.1 15.8 1.0 O B:HOH1112 2.1 21.6 1.0 O B:HOH1113 2.3 25.2 1.0 CE1 B:HIS98 2.8 20.8 1.0 CE1 B:HIS9 2.9 17.4 1.0 CD2 B:HIS98 3.0 19.9 1.0 CG B:HIS9 3.1 16.7 1.0 CB B:HIS9 3.5 15.1 1.0 ND1 B:HIS98 4.0 21.2 1.0 NE2 B:HIS9 4.0 16.1 1.0 CG B:HIS98 4.1 17.5 1.0 CD2 B:HIS9 4.1 18.3 1.0 N B:HIS9 4.3 14.2 1.0 NE B:ARG47 4.4 19.2 1.0 C B:VAL8 4.5 14.2 1.0 CA B:HIS9 4.6 14.4 1.0 O B:VAL8 4.6 15.4 1.0 CG B:ARG47 4.9 14.8 1.0 CG B:PRO100 4.9 15.4 1.0 NH2 B:ARG47 4.9 24.2 1.0

Zinc binding site 7 out of 18 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn


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 E.Coli Transthyretin-Related Protein with Bound Zn within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1006 b:40.9 occ:0.35 NE2 B:HIS96 2.4 18.9 0.3 O B:SER114 2.4 21.9 1.0 ZN B:ZN1010 2.6 50.4 0.3 CD2 B:HIS96 2.7 18.1 0.3 CE1 B:HIS96 3.0 19.9 0.7 ND1 B:HIS96 3.0 18.9 0.7 CG B:HIS98 3.1 17.5 1.0 CB B:HIS98 3.2 15.4 1.0 ND1 B:HIS98 3.2 21.2 1.0 C B:SER114 3.3 21.0 1.0 OXT B:SER114 3.5 22.2 1.0 CE1 B:HIS96 3.6 18.1 0.3 CD2 B:HIS98 3.9 19.9 1.0 CE1 B:HIS98 3.9 20.8 1.0 CG B:HIS96 4.0 17.9 0.3 NE2 B:HIS98 4.3 18.6 1.0 NE2 B:HIS96 4.3 19.0 0.7 CG B:HIS96 4.4 18.5 0.7 ND1 B:HIS96 4.4 18.2 0.3 CA B:HIS98 4.5 15.5 1.0 CA B:SER114 4.7 20.2 1.0 N B:SER114 4.9 18.9 1.0 N B:HIS98 5.0 15.5 1.0 CD2 B:HIS96 5.0 19.0 0.7

Zinc binding site 8 out of 18 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn


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 E.Coli Transthyretin-Related Protein with Bound Zn within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1010 b:50.4 occ:0.30 CD2 B:HIS96 2.1 18.1 0.3 OXT B:SER114 2.5 22.2 1.0 ZN B:ZN1006 2.6 40.9 0.3 ND1 B:HIS96 2.8 18.9 0.7 C B:SER114 3.1 21.0 1.0 CG B:HIS96 3.1 17.9 0.3 O B:SER114 3.1 21.9 1.0 NE2 B:HIS96 3.1 18.9 0.3 CG B:HIS96 3.6 18.5 0.7 CB B:HIS96 3.6 17.7 0.3 CB B:HIS96 3.7 17.8 0.7 CE1 B:HIS96 3.7 19.9 0.7 ND1 B:HIS96 4.2 18.2 0.3 CE1 B:HIS96 4.2 18.1 0.3 O B:HOH1111 4.3 31.5 1.0 CA B:SER114 4.3 20.2 1.0 CB B:HIS98 4.4 15.4 1.0 O B:HIS96 4.5 17.0 0.7 O B:HIS96 4.5 17.0 0.3 C B:HIS96 4.6 17.1 0.3 C B:HIS96 4.6 17.1 0.7 CA B:HIS96 4.8 17.6 0.3 CD2 B:HIS96 4.8 19.0 0.7 CA B:HIS96 4.8 17.7 0.7 NE2 B:HIS96 4.8 19.0 0.7 O B:GLY113 5.0 17.7 1.0

Zinc binding site 9 out of 18 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn


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 E.Coli Transthyretin-Related Protein with Bound Zn within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1014 b:30.1 occ:1.00 OD1 B:ASP61 1.9 15.2 1.0 ND1 B:HIS89 2.0 17.4 1.0 O B:HOH1114 2.3 25.4 1.0 CE1 B:HIS89 2.8 17.1 1.0 CG B:ASP61 3.0 14.4 1.0 CG B:HIS89 3.0 17.2 1.0 OD2 B:ASP61 3.3 14.8 1.0 CB B:HIS89 3.5 16.1 1.0 CA B:HIS89 3.9 16.6 1.0 NE2 B:HIS89 4.0 18.1 1.0 CD2 B:HIS89 4.1 17.9 1.0 C B:GLY60 4.2 12.8 1.0 CB B:ASP61 4.3 13.4 1.0 N B:ASP61 4.3 13.0 1.0 O B:GLY60 4.3 11.4 1.0 O B:HOH1175 4.3 32.7 1.0 CA B:ASP61 4.4 12.8 1.0 CA B:GLY60 4.7 13.3 1.0 N B:HIS89 4.8 15.9 1.0 C B:HIS89 5.0 17.1 1.0

Zinc binding site 10 out of 18 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn


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 E.Coli Transthyretin-Related Protein with Bound Zn within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1018 b:38.8 occ:0.60 OE2 B:GLU83 1.7 19.4 1.0 OE2 A:GLU87 1.8 19.5 1.0 O A:HOH1029 2.2 30.0 1.0 CD A:GLU87 2.6 17.9 1.0 OE1 A:GLU87 2.8 20.3 1.0 CD B:GLU83 2.8 17.2 1.0 CG B:GLU83 3.4 16.5 1.0 O A:HOH1089 3.8 40.0 1.0 OE1 B:GLU83 3.9 19.0 1.0 O B:HOH1167 3.9 34.5 1.0 CG A:GLU87 4.0 15.8 1.0 CZ2 A:TRP34 4.2 17.5 1.0 O B:HOH1136 4.2 38.1 1.0 O B:HOH1135 4.5 36.0 1.0 CG1 B:VAL65 4.5 14.7 1.0 CB B:GLU83 4.9 15.7 1.0 CH2 A:TRP34 4.9 18.2 1.0 CG B:PRO85 4.9 14.2 1.0 CD B:PRO85 5.0 14.3 1.0

E.Lundberg, S.Backstrom, U.H.Sauer, A.E.Sauer-Eriksson. The Transthyretin-Related Protein: Structural Investigation of A Novel Protein Family J.Struct.Biol. V. 155 445 2006.
ISSN: ISSN 1047-8477
PubMed: 16723258
DOI: 10.1016/J.JSB.2006.04.002