6XPE
Cryo-EM structure of human ZnT8 WT, in the presence of zinc, determined in outward-facing conformation
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006812 | biological_process | monoatomic cation transport |
A | 0008324 | molecular_function | monoatomic cation transmembrane transporter activity |
A | 0016020 | cellular_component | membrane |
A | 0055085 | biological_process | transmembrane transport |
B | 0006812 | biological_process | monoatomic cation transport |
B | 0008324 | molecular_function | monoatomic cation transmembrane transporter activity |
B | 0016020 | cellular_component | membrane |
B | 0055085 | biological_process | transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue ZN B 401 |
Chain | Residue |
A | CYS53 |
B | HIS301 |
B | HIS318 |
B | GLN350 |
B | GLU352 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue ZN B 402 |
Chain | Residue |
B | HIS137 |
B | HIS345 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue ZN B 403 |
Chain | Residue |
B | ASP224 |
B | HIS106 |
B | ASP110 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN A 401 |
Chain | Residue |
A | HIS52 |
A | HIS54 |
B | CYS361 |
B | CYS364 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue ZN A 402 |
Chain | Residue |
A | HIS301 |
A | HIS318 |
A | GLN350 |
A | GLU352 |
B | CYS53 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue ZN A 403 |
Chain | Residue |
A | CYS361 |
A | CYS364 |
B | HIS52 |
B | HIS54 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue ZN A 404 |
Chain | Residue |
A | HIS137 |
A | HIS345 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue ZN A 405 |
Chain | Residue |
A | HIS106 |
A | ASP110 |
A | ASP224 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 30 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"16984975","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 160 |
Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | Topological domain: {"description":"Lumenal, vesicle","evidences":[{"source":"PubMed","id":"16984975","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Motif: {"description":"HCH Motif; seals regulatory zinc-binding pocket","evidences":[{"source":"PubMed","id":"32723473","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | Binding site: {"description":"in chain A","evidences":[{"source":"PubMed","id":"32723473","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6XPE","evidenceCode":"ECO:0000312"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"32723473","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6XPE","evidenceCode":"ECO:0000312"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 10 |
Details | Binding site: {"description":"in chain B","evidences":[{"source":"PubMed","id":"32723473","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6XPE","evidenceCode":"ECO:0000312"}]} |
Chain | Residue | Details |