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1BTJ

HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE, APO FORM, CRYSTAL FORM 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
B0005576cellular_componentextracellular region
Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD
ChainResidueDetails
ATYR95-ASP104

site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF
ChainResidueDetails
ATYR188-PHE204

site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV
ChainResidueDetails
AGLN222-VAL252

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83
ChainResidueDetails
AASP63
ATYR95
ATYR188
AHIS249
BASP63
BTYR95
BTYR188
BHIS249

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ATHR120
AARG124
AALA126
AGLY127
BTHR120
BARG124
BALA126
BGLY127

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:P12346
ChainResidueDetails
AARG23
BARG23

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: O-linked (GalNAc...) serine
ChainResidueDetails
ASER32
BSER32

222624

PDB entries from 2024-07-17

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