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6UJ6

X-ray Crystal Structure of Chromium-transferrin with Synergistic Anion Malonate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0008199molecular_functionferric iron binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CR A 701
ChainResidue
AASP411
ATYR445
ATYR536
AHIS604
AMLI702

site_idAC2
Number of Residues10
Detailsbinding site for residue MLI A 702
ChainResidue
ATHR476
AALA477
AGLY478
ATYR536
AHIS604
ACR701
AASP411
ATYR445
ATHR471
AARG475

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL A 703
ChainResidue
ACYS246
ALEU247
AASP248
AASP259
ACYS260
AHIS261

site_idAC4
Number of Residues2
Detailsbinding site for residue GOL A 704
ChainResidue
AMET128
AASP157

site_idAC5
Number of Residues4
Detailsbinding site for residue BCT A 705
ChainResidue
AGLU429
AHIS604
ALEU649
AARG651

Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD
ChainResidueDetails
ATYR114-ASP123
ATYR445-SER454

site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF
ChainResidueDetails
ATYR207-PHE223
ATYR536-PHE551

site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV
ChainResidueDetails
AGLN241-VAL271
AASP577-VAL607

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Dimethylated arginine","evidences":[{"source":"UniProtKB","id":"P12346","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GalNAc...) serine","featureId":"CAR_000073"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000074","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15536627","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31636418","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6SOY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6SOZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; atypical; partial","evidences":[{"source":"PubMed","id":"15536627","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000075","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15536627","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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