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8XV5

Pyridoxamine-bound human SLC19A3

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0009055molecular_functionelectron transfer activity
A0009229biological_processthiamine diphosphate biosynthetic process
A0015234molecular_functionthiamine transmembrane transporter activity
A0015888biological_processthiamine transport
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0031923biological_processpyridoxine transport
A0042597cellular_componentperiplasmic space
A0042723biological_processthiamine-containing compound metabolic process
A0046872molecular_functionmetal ion binding
A0051180biological_processvitamin transport
A0055085biological_processtransmembrane transport
A0071934biological_processthiamine transmembrane transport
A0090482molecular_functionvitamin transmembrane transporter activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ATRP-89
AILE6

site_idSWS_FT_FI2
Number of Residues64
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AARG29-ASN53
AVAL103-GLU110
AASN166-TYR169
AASP304-ASN316
AHIS364-GLY375
AASP427-PRO434

site_idSWS_FT_FI3
Number of Residues220
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AGLU54-THR74
AVAL406-VAL426
AVAL435-MET455
AVAL82-GLY102
APHE111-VAL131
ASER145-ALA165
APHE170-LEU190
ALEU283-TRP303
AGLY317-VAL337
ALEU343-MET363
ATYR376-VAL396

site_idSWS_FT_FI4
Number of Residues161
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AASP75-PRO81
ASER132-ARG144
APRO191-SER282
ALYS338-ASP342
AASN397-LEU405
AARG456-LEU496

site_idSWS_FT_FI5
Number of Residues7
DetailsSITE: Essential for pyridoxine transport => ECO:0000269|PubMed:35724964
ChainResidueDetails
AGLN86
AGLY87
AILE91
ATHR93
ATRP94
ASER168
AASN173

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN45

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN166

222926

PDB entries from 2024-07-24

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