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6XPF

Cryo-EM structure of human ZnT8 WT, in the absence of zinc, determined in heterogeneous conformations- one subunit in an inward-facing and the other in an outward-facing conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0006812biological_processmonoatomic cation transport
A0008324molecular_functionmonoatomic cation transmembrane transporter activity
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
B0006812biological_processmonoatomic cation transport
B0008324molecular_functionmonoatomic cation transmembrane transporter activity
B0016020cellular_componentmembrane
B0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue ZN A 401
ChainResidue
AASP360
ACYS361

site_idAC2
Number of Residues1
Detailsbinding site for residue ZN A 402
ChainResidue
ACYS53

site_idAC3
Number of Residues1
Detailsbinding site for residue ZN B 402
ChainResidue
BCYS361

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues226
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:16984975
ChainResidueDetails
AMET50-PRO128
AGLN174-ASN189
AILE246-ILE266
BMET50-PRO128
BGLN174-ASN189
BILE246-ILE266

site_idSWS_FT_FI2
Number of Residues240
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
ASER129-LEU149
BLEU225-LYS245
BLEU267-VAL287
BASP295-LEU315
AVAL153-ILE173
AILE190-ALA210
ALEU225-LYS245
ALEU267-VAL287
AASP295-LEU315
BSER129-LEU149
BVAL153-ILE173
BILE190-ALA210

site_idSWS_FT_FI3
Number of Residues42
DetailsTOPO_DOM: Lumenal, vesicle => ECO:0000269|PubMed:16984975
ChainResidueDetails
ACYS150-TRP152
AASN211-ASP224
ALYS288-VAL294
BCYS150-TRP152
BASN211-ASP224
BLYS288-VAL294

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: in chain A => ECO:0000269|PubMed:32723473, ECO:0000312|PDB:6XPE
ChainResidueDetails
AVAL101
ATHR102
AASP103
BVAL101
BTHR102
BASP103

site_idSWS_FT_FI5
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:32723473, ECO:0000312|PDB:6XPE
ChainResidueDetails
ATHR155
BLEU273
AVAL159
AVAL186
AASP269
ALEU273
BTHR155
BVAL159
BVAL186
BASP269

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: in chain B => ECO:0000269|PubMed:32723473, ECO:0000312|PDB:6XPE
ChainResidueDetails
AGLN350
APRO367
BGLN350
BPRO367

237735

PDB entries from 2025-06-18

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