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1JQF

Human Transferrin N-Lobe Mutant H249Q

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CO3 A 600
ChainResidue
AASP63
AFE500
ATYR95
ATHR120
AARG124
ASER125
AALA126
AGLY127
ATYR188
AGLN249

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 500
ChainResidue
AASP63
ATYR95
ATYR188
AGLN249
ACO3600

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 701
ChainResidue
AALA151
AASN152
APHE154
AGLN169
AHOH821

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...VdeykdChlAqvpsQtVV
ChainResidueDetails
AGLN222-VAL252

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22327295, ECO:0007744|PDB:3V83
ChainResidueDetails
AASP63
ATYR95
ATYR188
AGLN249

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ATHR120
AARG124
AALA126
AGLY127

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:P12346
ChainResidueDetails
AARG23

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: O-linked (GalNAc...) serine
ChainResidueDetails
ASER32

225946

PDB entries from 2024-10-09

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