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8ZSB

Cryo-EM structure of human ZnT1, in the absence of zinc, determined in outward-facing conformation

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues640
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:31471319
ChainResidueDetails
AMET1-ARG10
AALA57-GLU78
AHIS135-VAL248
ATYR330-LEU507
BMET1-ARG10
BALA57-GLU78
BHIS135-VAL248
BTYR330-LEU507

site_idSWS_FT_FI2
Number of Residues240
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
ALEU11-VAL31
BLEU114-PHE134
BPHE249-PHE269
BGLY309-LEU329
AALA36-VAL56
AVAL79-GLU99
ALEU114-PHE134
APHE249-PHE269
AGLY309-LEU329
BLEU11-VAL31
BALA36-VAL56
BVAL79-GLU99

site_idSWS_FT_FI3
Number of Residues108
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:31471319
ChainResidueDetails
ATHR32-LEU35
AALA100-PRO113
ATYR270-ALA308
BTHR32-LEU35
BALA100-PRO113
BTYR270-ALA308

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q62720
ChainResidueDetails
AHIS43
AASP255
BHIS43
BASP255

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P69380
ChainResidueDetails
AASP47
AHIS251
BASP47
BHIS251

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER506
BSER506

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31471319
ChainResidueDetails
AASN299
BASN299

224004

PDB entries from 2024-08-21

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