Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
A0006826biological_processiron ion transport
A0046872molecular_functionmetal ion binding
A0055037cellular_componentrecycling endosome
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005769cellular_componentearly endosome
B0005886cellular_componentplasma membrane
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 Residues14
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741
ChainResidueDetails
AASP57
BTHR116
BARG120
BVAL122
BGLY123
BTYR204
ATYR90
ATHR116
AARG120
AVAL122
AGLY123
ATYR204
BASP57
BTYR90

site_idSWS_FT_FI2
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN200
AASN337
AASN400
BASN200
BASN337
BASN400

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon