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3SKP

The structure of apo-human transferrin C-lobe with bound sulfate ions

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AHOH45
AHOH299
AHOH327
AARG456
ATHR457

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 680
ChainResidue
AHIS350
AARG475
ATHR626
AHOH39
AHOH111
AHOH155
ASER348

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 681
ChainResidue
AHOH217
AHOH306
AHIS349
AARG352
ASER370
AHIS473

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 682
ChainResidue
ALYS365
APRO422
AHIS642
AASP643
AARG644

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 683
ChainResidue
AHOH18
AHOH20
AHOH53
AHOH296
AHIS578
AALA580
AARG581
AGLY652
AGLU653
AGLU654
ATYR655

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 684
ChainResidue
AHOH147
AHOH253
AHOH325
AGLN536
AGLN540
AASN618

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 685
ChainResidue
AHOH162
AGLY516
ATYR517
ATHR518
AHOH690
AHOH715

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 686
ChainResidue
AHOH96
AALA595
AHIS598
ALYS640

Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YfAVAVVKKS
ChainResidueDetails
ATYR426-SER435

site_idPS00206
Number of Residues16
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YtGAFRCLvek.GDVAF
ChainResidueDetails
ATYR517-PHE532

site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. DYeLLClDgtrkp...VeeyanChlArapnHaVV
ChainResidueDetails
AASP558-VAL588

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues322
DetailsDomain: {"description":"Transferrin-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343719","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31636418","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VE1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6SOY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6SOZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
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_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; atypical; partial","evidences":[{"source":"PubMed","id":"15536627","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
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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