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6WB6

2.05 A resolution structure of transferrin 1 from Manduca sexta

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005769cellular_componentearly endosome
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006826biological_processiron ion transport
A0046872molecular_functionmetal ion binding
A0055037cellular_componentrecycling endosome
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005769cellular_componentearly endosome
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006826biological_processiron ion transport
B0046872molecular_functionmetal ion binding
B0055037cellular_componentrecycling endosome
Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YeAVIVVHKD
ChainResidueDetails
ATYR90-ASP99
ATYR437-GLY445

site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YeGALRCLahnnGEVAF
ChainResidueDetails
ATYR204-PHE220

site_idPS00207
Number of Residues30
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. EFrYLCvDgskap...Itgka.CswAarpwQgLI
ChainResidueDetails
AGLU248-ILE277
AGLN556-VAL589

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues682
DetailsDomain: {"description":"Transferrin-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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