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9FQW

Cryo-EM structure of MmCAT1 bound with FrMLV-RBD in the ornithine-bound inward-occluded state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000064molecular_functionL-ornithine transmembrane transporter activity
A0001618molecular_functionvirus receptor activity
A0005290molecular_functionL-histidine transmembrane transporter activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006865biological_processamino acid transport
A0009925cellular_componentbasal plasma membrane
A0015171molecular_functionamino acid transmembrane transporter activity
A0015174molecular_functionbasic amino acid transmembrane transporter activity
A0015189molecular_functionL-lysine transmembrane transporter activity
A0015807biological_processL-amino acid transport
A0015819biological_processlysine transport
A0015822biological_processornithine transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0032006biological_processregulation of TOR signaling
A0032991cellular_componentprotein-containing complex
A0042102biological_processpositive regulation of T cell proliferation
A0046718biological_processsymbiont entry into host cell
A0061459molecular_functionL-arginine transmembrane transporter activity
A0089718biological_processamino acid import across plasma membrane
A0097638biological_processL-arginine import across plasma membrane
A1903352biological_processL-ornithine transmembrane transport
A1903401biological_processL-lysine transmembrane transport
A1903810biological_processL-histidine import across plasma membrane
A1903826biological_processL-arginine transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues284
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues113
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues77
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host"}
ChainResidueDetails

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PDB entries from 2025-10-08

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