Zinc in PDB 6r8n: Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A

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>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 24;

Binding sites:

The binding sites of Zinc atom in the Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A (pdb code 6r8n). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 24 binding sites of Zinc where determined in the Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A, PDB code: 6r8n:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 24 in the Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:20.0 occ:1.00 OE1 A:GLU213 2.0 20.0 1.0 CD A:GLU213 2.9 20.0 1.0 OE2 A:GLU213 3.2 20.0 1.0 NE2 A:HIS68 3.2 20.0 1.0 OD1 A:ASP182 3.4 20.0 1.0 O A:VAL236 3.7 20.0 1.0 OD2 A:ASP182 3.8 20.0 1.0 HD2 A:HIS68 3.9 20.0 1.0 CD2 A:HIS68 3.9 20.0 1.0 OD1 A:ASP235 3.9 20.0 1.0 CG A:ASP182 4.0 20.0 1.0 CE1 A:HIS68 4.3 20.0 1.0 CG A:GLU213 4.4 20.0 1.0 HH11 A:ARG320 4.4 20.0 1.0 HE1 A:HIS68 4.5 20.0 1.0 HG2 A:GLU213 4.6 20.0 1.0 HB A:THR237 4.6 20.0 1.0 H A:VAL236 4.6 20.0 1.0 OD2 A:ASP183 4.6 20.0 1.0 HG3 A:GLU213 4.6 20.0 1.0 HH12 A:ARG320 4.6 20.0 1.0 OD2 A:ASP235 4.8 20.0 1.0 CG A:ASP235 4.8 20.0 1.0 NH1 A:ARG320 4.8 20.0 1.0 C A:VAL236 4.9 20.0 1.0

Zinc binding site 2 out of 24 in the Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1002 b:20.0 occ:1.00 H A:GLY297 4.0 20.0 1.0 HA2 A:GLY92 4.2 20.0 1.0 HA2 A:GLY296 4.4 20.0 1.0 N A:GLY297 4.6 20.0 1.0 O A:GLU213 4.7 20.0 1.0 HA3 A:GLY297 4.7 20.0 1.0 HA3 A:GLY92 4.8 20.0 1.0 CA A:GLY92 4.9 20.0 1.0 HG3 A:GLU213 4.9 20.0 1.0

Zinc binding site 3 out of 24 in the Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1001 b:20.0 occ:1.00 OE1 B:GLU213 2.0 20.0 1.0 CD B:GLU213 2.9 20.0 1.0 OE2 B:GLU213 3.2 20.0 1.0 NE2 B:HIS68 3.2 20.0 1.0 OD1 B:ASP182 3.4 20.0 1.0 O B:VAL236 3.7 20.0 1.0 OD2 B:ASP182 3.8 20.0 1.0 HD2 B:HIS68 3.9 20.0 1.0 CD2 B:HIS68 3.9 20.0 1.0 OD1 B:ASP235 3.9 20.0 1.0 CG B:ASP182 4.0 20.0 1.0 CE1 B:HIS68 4.3 20.0 1.0 CG B:GLU213 4.4 20.0 1.0 HH11 B:ARG320 4.4 20.0 1.0 HE1 B:HIS68 4.5 20.0 1.0 HG2 B:GLU213 4.6 20.0 1.0 HB B:THR237 4.6 20.0 1.0 H B:VAL236 4.6 20.0 1.0 OD2 B:ASP183 4.6 20.0 1.0 HG3 B:GLU213 4.6 20.0 1.0 HH12 B:ARG320 4.7 20.0 1.0 OD2 B:ASP235 4.8 20.0 1.0 CG B:ASP235 4.8 20.0 1.0 NH1 B:ARG320 4.8 20.0 1.0 C B:VAL236 4.9 20.0 1.0

Zinc binding site 4 out of 24 in the Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1002 b:20.0 occ:1.00 H B:GLY297 4.0 20.0 1.0 HA2 B:GLY92 4.2 20.0 1.0 HA2 B:GLY296 4.4 20.0 1.0 N B:GLY297 4.6 20.0 1.0 O B:GLU213 4.7 20.0 1.0 HA3 B:GLY297 4.7 20.0 1.0 HA3 B:GLY92 4.8 20.0 1.0 CA B:GLY92 4.9 20.0 1.0 HG3 B:GLU213 4.9 20.0 1.0

Zinc binding site 5 out of 24 in the Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1001 b:20.0 occ:1.00 OE1 C:GLU213 2.0 20.0 1.0 CD C:GLU213 2.9 20.0 1.0 OE2 C:GLU213 3.2 20.0 1.0 NE2 C:HIS68 3.2 20.0 1.0 OD1 C:ASP182 3.4 20.0 1.0 O C:VAL236 3.7 20.0 1.0 OD2 C:ASP182 3.8 20.0 1.0 HD2 C:HIS68 3.9 20.0 1.0 CD2 C:HIS68 3.9 20.0 1.0 OD1 C:ASP235 3.9 20.0 1.0 CG C:ASP182 4.0 20.0 1.0 CE1 C:HIS68 4.3 20.0 1.0 CG C:GLU213 4.4 20.0 1.0 HH11 C:ARG320 4.4 20.0 1.0 HE1 C:HIS68 4.5 20.0 1.0 HG2 C:GLU213 4.6 20.0 1.0 HB C:THR237 4.6 20.0 1.0 H C:VAL236 4.6 20.0 1.0 OD2 C:ASP183 4.6 20.0 1.0 HG3 C:GLU213 4.6 20.0 1.0 HH12 C:ARG320 4.7 20.0 1.0 OD2 C:ASP235 4.8 20.0 1.0 CG C:ASP235 4.8 20.0 1.0 NH1 C:ARG320 4.8 20.0 1.0 C C:VAL236 4.9 20.0 1.0

Zinc binding site 6 out of 24 in the Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1002 b:20.0 occ:1.00 H C:GLY297 4.0 20.0 1.0 HA2 C:GLY92 4.2 20.0 1.0 HA2 C:GLY296 4.4 20.0 1.0 N C:GLY297 4.6 20.0 1.0 O C:GLU213 4.7 20.0 1.0 HA3 C:GLY297 4.7 20.0 1.0 HA3 C:GLY92 4.8 20.0 1.0 CA C:GLY92 4.9 20.0 1.0 HG3 C:GLU213 4.9 20.0 1.0

Zinc binding site 7 out of 24 in the Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1001 b:20.0 occ:1.00 OE1 D:GLU213 2.0 20.0 1.0 CD D:GLU213 2.9 20.0 1.0 OE2 D:GLU213 3.2 20.0 1.0 NE2 D:HIS68 3.2 20.0 1.0 OD1 D:ASP182 3.4 20.0 1.0 O D:VAL236 3.7 20.0 1.0 OD2 D:ASP182 3.8 20.0 1.0 HD2 D:HIS68 3.9 20.0 1.0 CD2 D:HIS68 3.9 20.0 1.0 OD1 D:ASP235 3.9 20.0 1.0 CG D:ASP182 4.0 20.0 1.0 CE1 D:HIS68 4.3 20.0 1.0 CG D:GLU213 4.4 20.0 1.0 HH11 D:ARG320 4.4 20.0 1.0 HE1 D:HIS68 4.5 20.0 1.0 HG2 D:GLU213 4.6 20.0 1.0 H D:VAL236 4.6 20.0 1.0 OD2 D:ASP183 4.6 20.0 1.0 HG3 D:GLU213 4.6 20.0 1.0 HH12 D:ARG320 4.7 20.0 1.0 OD2 D:ASP235 4.8 20.0 1.0 CG D:ASP235 4.8 20.0 1.0 NH1 D:ARG320 4.8 20.0 1.0 C D:VAL236 4.9 20.0 1.0

Zinc binding site 8 out of 24 in the Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1002 b:20.0 occ:1.00 H D:GLY297 4.0 20.0 1.0 HA2 D:GLY92 4.2 20.0 1.0 HA2 D:GLY296 4.4 20.0 1.0 N D:GLY297 4.6 20.0 1.0 O D:GLU213 4.7 20.0 1.0 HA3 D:GLY297 4.7 20.0 1.0 HA3 D:GLY92 4.8 20.0 1.0 CA D:GLY92 4.9 20.0 1.0 HG3 D:GLU213 4.9 20.0 1.0

Zinc binding site 9 out of 24 in the Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn1001 b:20.0 occ:1.00 OE1 E:GLU213 2.0 20.0 1.0 CD E:GLU213 2.9 20.0 1.0 OE2 E:GLU213 3.2 20.0 1.0 NE2 E:HIS68 3.2 20.0 1.0 OD1 E:ASP182 3.4 20.0 1.0 O E:VAL236 3.7 20.0 1.0 OD2 E:ASP182 3.8 20.0 1.0 HD2 E:HIS68 3.9 20.0 1.0 CD2 E:HIS68 3.9 20.0 1.0 OD1 E:ASP235 3.9 20.0 1.0 CG E:ASP182 4.0 20.0 1.0 CE1 E:HIS68 4.3 20.0 1.0 CG E:GLU213 4.4 20.0 1.0 HH11 E:ARG320 4.4 20.0 1.0 HE1 E:HIS68 4.5 20.0 1.0 HG2 E:GLU213 4.6 20.0 1.0 HB E:THR237 4.6 20.0 1.0 H E:VAL236 4.6 20.0 1.0 OD2 E:ASP183 4.6 20.0 1.0 HG3 E:GLU213 4.6 20.0 1.0 HH12 E:ARG320 4.7 20.0 1.0 OD2 E:ASP235 4.8 20.0 1.0 CG E:ASP235 4.8 20.0 1.0 NH1 E:ARG320 4.8 20.0 1.0 C E:VAL236 4.9 20.0 1.0

Zinc binding site 10 out of 24 in the Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Structure Determination of the Tetrahedral Aminopeptidase TET2 From P. Horikoshii By Use of Combined Solid-State uc(Nmr), Solution-State uc(Nmr) and Em Data 4.1 A, Followed By REAL_SPACE_REFINEMENT at 4.1 A within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn1002 b:20.0 occ:1.00 H E:GLY297 4.0 20.0 1.0 HA2 E:GLY92 4.2 20.0 1.0 HA2 E:GLY296 4.4 20.0 1.0 N E:GLY297 4.6 20.0 1.0 O E:GLU213 4.7 20.0 1.0 HA3 E:GLY297 4.7 20.0 1.0 HA3 E:GLY92 4.8 20.0 1.0 CA E:GLY92 4.9 20.0 1.0 HG3 E:GLU213 4.9 20.0 1.0

D.F.Gauto, L.F.Estrozi, C.D.Schwieters, G.Effantin, P.Macek, R.Sounier, A.C.Sivertsen, E.Schmidt, R.Kerfah, G.Mas, J.P.Colletier, P.Guntert, A.Favier, G.Schoehn, P.Schanda, J.Boisbouvier. Integrated uc(Nmr) and Cryo-Em Atomic-Resolution Structure Determination of A Half-Megadalton Enzyme Complex. Nat Commun V. 10 2697 2019.
ISSN: ESSN 2041-1723
PubMed: 31217444
DOI: 10.1038/S41467-019-10490-9