Zinc in PDB 2g2p: Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn and Br

The structure of Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn and Br, PDB code: 2g2p 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)	17.38 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.720, 92.030, 57.490, 90.00, 103.50, 90.00
R / Rfree (%)	17.5 / 22.9

The structure of Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn and Br also contains other interesting chemical elements:

Bromine

(Br)

4 atoms

Pages:

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

Binding sites:

The binding sites of Zinc atom in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn and Br (pdb code 2g2p). 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 E.Coli Transthyretin-Related Protein with Bound Zn and Br, PDB code: 2g2p:
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 E.Coli Transthyretin-Related Protein with Bound Zn and Br


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 and Br within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:48.3 occ:0.80 NE2 A:HIS98 1.9 29.0 1.0 ND1 A:HIS9 2.1 24.8 1.0 CE1 A:HIS98 2.3 30.6 1.0 O A:HOH1109 2.4 39.6 1.0 BR A:BR1021 2.6 52.4 0.9 CE1 A:HIS9 3.0 24.8 1.0 CG A:HIS9 3.1 22.9 1.0 CD2 A:HIS98 3.2 27.7 1.0 CB A:HIS9 3.5 21.0 1.0 ND1 A:HIS98 3.6 31.5 1.0 CG A:HIS98 4.1 25.1 1.0 NE2 A:HIS9 4.1 25.1 1.0 CD2 A:HIS9 4.2 24.9 1.0 N A:HIS9 4.4 20.9 1.0 C A:VAL8 4.6 20.1 1.0 O1 A:SO41102 4.6 46.2 0.7 CA A:HIS9 4.6 20.7 1.0 O A:VAL8 4.7 19.7 1.0 O A:HOH1141 4.7 46.2 1.0 ZN A:ZN1005 4.8 45.8 0.6 CG A:ARG47 4.8 19.0 1.0

Zinc binding site 2 out of 15 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn and Br


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 and Br within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1005 b:45.8 occ:0.55 ND1 A:HIS98 1.8 31.5 1.0 NE2 A:HIS96 2.2 24.9 0.6 O A:HOH1141 2.3 46.2 1.0 CE1 A:HIS96 2.3 24.8 0.5 CE1 A:HIS98 2.6 30.6 1.0 CG A:HIS98 2.8 25.1 1.0 O A:SER114 3.0 25.1 1.0 ND1 A:HIS96 3.2 24.3 0.5 CD2 A:HIS96 3.2 24.2 0.6 CE1 A:HIS96 3.3 24.9 0.6 CB A:HIS98 3.3 22.6 1.0 NE2 A:HIS96 3.4 24.6 0.5 NE2 A:HIS98 3.7 29.0 1.0 CD2 A:HIS98 3.8 27.7 1.0 ZN A:ZN1009 4.0 54.8 0.5 CB A:SER7 4.0 18.5 1.0 C A:SER114 4.1 25.6 1.0 OG A:SER7 4.2 18.8 1.0 CG A:HIS96 4.3 23.4 0.6 ND1 A:HIS96 4.4 24.6 0.6 CG A:HIS96 4.4 23.2 0.5 CA A:HIS98 4.5 21.8 1.0 CD2 A:HIS96 4.5 24.2 0.5 OXT A:SER114 4.6 27.2 1.0 ZN A:ZN1001 4.8 48.3 0.8

Zinc binding site 3 out of 15 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn and Br


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 and Br within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1009 b:54.8 occ:0.45 OXT A:SER114 2.1 27.2 1.0 CD2 A:HIS96 2.1 24.2 0.6 ND1 A:HIS96 2.3 24.3 0.5 C A:SER114 2.8 25.6 1.0 O A:SER114 2.8 25.1 1.0 CG A:HIS96 3.0 23.4 0.6 NE2 A:HIS96 3.2 24.9 0.6 CG A:HIS96 3.2 23.2 0.5 CE1 A:HIS96 3.4 24.8 0.5 CB A:HIS96 3.4 22.2 0.5 CB A:HIS96 3.5 22.2 0.6 ZN A:ZN1005 4.0 45.8 0.6 ND1 A:HIS96 4.2 24.6 0.6 CA A:SER114 4.2 25.4 1.0 CE1 A:HIS96 4.3 24.9 0.6 O A:HIS96 4.3 21.7 0.6 CD2 A:HIS96 4.4 24.2 0.5 NE2 A:HIS96 4.4 24.6 0.5 O A:HOH1108 4.5 34.4 1.0 O A:HIS96 4.5 21.6 0.5 C A:HIS96 4.6 21.6 0.6 CA A:HIS96 4.7 22.2 0.6 CA A:HIS96 4.7 22.1 0.5 C A:HIS96 4.7 21.6 0.5

Zinc binding site 4 out of 15 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn and Br


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 and Br within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1013 b:58.1 occ:0.55 OD1 A:ASP61 2.0 26.8 1.0 ND1 A:HIS89 2.1 26.7 1.0 O A:HOH1136 2.5 52.5 1.0 CE1 A:HIS89 2.7 25.9 1.0 CG A:HIS89 2.7 23.4 1.0 CG A:ASP61 3.1 22.1 1.0 CB A:HIS89 3.4 20.6 1.0 NE2 A:HIS89 3.4 26.9 1.0 CD2 A:HIS89 3.5 26.5 1.0 OD2 A:ASP61 3.5 25.0 1.0 C A:GLY60 3.8 20.8 1.0 N A:ASP61 3.9 20.1 1.0 CA A:HIS89 4.1 20.7 1.0 O A:GLY60 4.1 20.2 1.0 CA A:GLY60 4.1 21.4 1.0 CB A:ASP61 4.2 20.8 1.0 CA A:ASP61 4.2 20.0 1.0 O B:HOH1117 4.6 55.7 1.0 CB B:PRO82 4.8 20.1 1.0 N A:GLY60 4.9 22.1 1.0

Zinc binding site 5 out of 15 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn and Br


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 and Br within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1002 b:47.9 occ:0.80 NE2 B:HIS98 1.9 26.0 1.0 ND1 B:HIS9 2.2 26.4 1.0 CE1 B:HIS98 2.4 28.8 1.0 O B:HOH1115 2.4 41.6 1.0 BR B:BR1022 2.5 49.5 0.8 CE1 B:HIS9 3.0 28.8 1.0 CG B:HIS9 3.2 23.6 1.0 CD2 B:HIS98 3.2 26.1 1.0 CB B:HIS9 3.6 21.2 1.0 ND1 B:HIS98 3.7 29.3 1.0 NE2 B:HIS9 4.1 27.1 1.0 CG B:HIS98 4.1 24.9 1.0 CD2 B:HIS9 4.2 25.2 1.0 O1 B:SO41104 4.3 42.0 0.5 N B:HIS9 4.3 19.8 1.0 C B:VAL8 4.4 20.1 1.0 O B:VAL8 4.5 20.1 1.0 CA B:HIS9 4.6 20.2 1.0 O B:HOH1141 4.6 50.3 1.0 NE B:ARG47 4.6 26.5 1.0 CG B:ARG47 4.8 18.8 1.0

Zinc binding site 6 out of 15 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn and Br


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 and Br within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1006 b:49.3 occ:0.60 ND1 B:HIS98 1.9 29.3 1.0 CE1 B:HIS96 2.4 24.1 0.4 O B:SER114 2.4 24.6 1.0 NE2 B:HIS96 2.5 26.2 0.6 O B:HOH1141 2.6 50.3 1.0 CG B:HIS98 2.8 24.9 1.0 CE1 B:HIS98 2.8 28.8 1.0 CD2 B:HIS96 3.0 25.1 0.6 ND1 B:HIS96 3.0 23.8 0.4 ZN B:ZN1010 3.1 60.5 0.4 CB B:HIS98 3.2 22.7 1.0 C B:SER114 3.6 24.9 1.0 NE2 B:HIS96 3.6 24.0 0.4 CE1 B:HIS96 3.8 26.0 0.6 NE2 B:HIS98 3.9 26.0 1.0 CD2 B:HIS98 3.9 26.1 1.0 OXT B:SER114 4.1 26.4 1.0 CG B:HIS96 4.3 24.0 0.6 CG B:HIS96 4.3 22.9 0.4 CA B:HIS98 4.5 22.6 1.0 CD2 B:HIS96 4.6 23.6 0.4 CB B:SER7 4.6 19.3 1.0 OG B:SER7 4.6 18.0 1.0 ND1 B:HIS96 4.7 25.6 0.6 CA B:SER114 4.9 24.6 1.0 N B:SER114 5.0 23.0 1.0

Zinc binding site 7 out of 15 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn and Br


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 and Br within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1010 b:60.5 occ:0.40 CD2 B:HIS96 2.2 25.1 0.6 ND1 B:HIS96 2.2 23.8 0.4 OXT B:SER114 2.5 26.4 1.0 O B:SER114 2.7 24.6 1.0 C B:SER114 2.8 24.9 1.0 CG B:HIS96 3.1 24.0 0.6 ZN B:ZN1006 3.1 49.3 0.6 CE1 B:HIS96 3.2 24.1 0.4 NE2 B:HIS96 3.2 26.2 0.6 CG B:HIS96 3.2 22.9 0.4 CB B:HIS96 3.5 22.1 0.6 CB B:HIS96 3.6 21.8 0.4 CA B:SER114 4.2 24.6 1.0 ND1 B:HIS96 4.3 25.6 0.6 O B:HIS96 4.3 20.9 0.6 NE2 B:HIS96 4.3 24.0 0.4 CE1 B:HIS96 4.3 26.0 0.6 O B:HIS96 4.3 21.0 0.4 CD2 B:HIS96 4.4 23.6 0.4 O B:HOH1112 4.4 30.2 1.0 CB B:HIS98 4.5 22.7 1.0 C B:HIS96 4.5 21.4 0.6 C B:HIS96 4.5 21.3 0.4 ND1 B:HIS98 4.6 29.3 1.0 O B:HOH1150 4.6 47.9 1.0 CA B:HIS96 4.6 21.8 0.6 CA B:HIS96 4.7 21.6 0.4 O B:GLY113 4.8 22.1 1.0 N B:SER114 5.0 23.0 1.0

Zinc binding site 8 out of 15 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn and Br


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 and Br within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1014 b:30.7 occ:1.00 OD1 B:ASP61 1.9 17.7 1.0 O B:HOH1144 2.1 24.0 1.0 ND1 B:HIS89 2.2 26.6 1.0 CE1 B:HIS89 2.8 27.2 1.0 CG B:ASP61 2.9 18.6 1.0 CG B:HIS89 3.0 23.3 1.0 OD2 B:ASP61 3.2 19.9 1.0 CB B:HIS89 3.5 20.4 1.0 NE2 B:HIS89 3.7 26.8 1.0 CD2 B:HIS89 3.8 28.1 1.0 CA B:HIS89 3.9 20.2 1.0 O B:GLY60 4.1 15.7 1.0 CB B:ASP61 4.3 16.7 1.0 C B:GLY60 4.4 16.0 1.0 N B:ASP61 4.5 16.0 1.0 OD1 B:ASN91 4.6 31.7 1.0 CA B:ASP61 4.6 16.7 1.0 N B:HIS89 4.8 19.5 1.0 N B:ILE90 5.0 20.4 1.0 C B:HIS89 5.0 20.0 1.0

Zinc binding site 9 out of 15 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn and Br


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 and Br within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1003 b:49.3 occ:0.55 ND1 C:HIS9 2.1 23.2 1.0 O C:HOH1109 2.1 39.4 1.0 NE2 C:HIS98 2.2 19.2 1.0 BR C:BR1023 2.5 51.5 0.7 CE1 C:HIS98 2.8 20.8 1.0 CG C:HIS9 2.9 22.6 1.0 CE1 C:HIS9 3.1 23.8 1.0 CB C:HIS9 3.2 21.0 1.0 CD2 C:HIS98 3.4 21.1 1.0 N C:HIS9 4.0 21.1 1.0 CD2 C:HIS9 4.0 23.4 1.0 ND1 C:HIS98 4.0 20.3 1.0 NE2 C:HIS9 4.1 23.9 1.0 C C:VAL8 4.1 20.2 1.0 O C:VAL8 4.1 20.0 1.0 CA C:HIS9 4.2 21.1 1.0 CG C:ARG47 4.3 23.1 1.0 CG C:HIS98 4.4 18.8 1.0 CD C:ARG47 4.5 24.0 1.0 NE C:ARG47 4.6 26.5 1.0 CA C:VAL8 4.9 20.1 1.0 CB C:SER7 5.0 19.1 1.0

Zinc binding site 10 out of 15 in the Crystal Structure of E.Coli Transthyretin-Related Protein with Bound Zn and Br


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 and Br within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1007 b:42.5 occ:1.00 O C:SER114 1.8 18.1 1.0 ND1 C:HIS98 1.9 20.3 1.0 NE2 C:HIS96 2.2 19.9 1.0 CG C:HIS98 2.8 18.8 1.0 CE1 C:HIS98 2.9 20.8 1.0 C C:SER114 2.9 19.3 1.0 CE1 C:HIS96 3.1 19.5 1.0 CB C:HIS98 3.1 18.6 1.0 OXT C:SER114 3.3 19.8 1.0 CD2 C:HIS96 3.3 21.1 1.0 CD2 C:HIS98 3.9 21.1 1.0 NE2 C:HIS98 3.9 19.2 1.0 CA C:SER114 4.2 19.6 1.0 ND1 C:HIS96 4.3 18.3 1.0 N C:SER114 4.4 19.7 1.0 CG C:HIS96 4.4 20.5 1.0 CA C:HIS98 4.5 18.8 1.0 OG C:SER7 4.9 18.7 1.0 C C:GLY113 4.9 20.5 1.0 CB C:SER7 5.0 19.1 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