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1DOT

CRYSTALLOGRAPHIC STRUCTURE OF DUCK OVOTRANSFERRIN AT 2.3 ANGSTROMS RESOLUTION

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
A0019731biological_processantibacterial humoral response
A0046872molecular_functionmetal ion binding
A0055037cellular_componentrecycling endosome
Functional Information from PDB Data
site_idFEC
Number of Residues7
DetailsIRON BINDING SITE IN THE C-LOBE
ChainResidue
ATYR431
ATYR524
AHIS592
AARG460
ACO3690
AFE688
AASP395

site_idFEN
Number of Residues7
DetailsIRON BINDING SITE IN THE N-LOBE
ChainResidue
AFE687
AASP60
ATYR92
ATYR191
AHIS250
AARG121
ACO3689

Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG
ChainResidueDetails
ATYR92-GLY101
ATYR431-SER440

site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFQCLkdgkGDVAF
ChainResidueDetails
ATYR191-PHE207
ATYR524-PHE539

site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. EYeLLClDgsrqp...VdsyktCnwArvaaHaVV
ChainResidueDetails
AGLU223-VAL253

site_idPS00962
Number of Residues12
DetailsRIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. VpELMDSQLYLG
ChainResidueDetails
AVAL310-GLY321

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN473
AASN548

218500

PDB entries from 2024-04-17

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