Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

9H49

Crystal structure of the adduct between human serum transferrin (apo-form) and cisplatin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005768	cellular_component	endosome
A	0005769	cellular_component	early endosome
A	0005770	cellular_component	late endosome
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005886	cellular_component	plasma membrane
A	0005905	cellular_component	clathrin-coated pit
A	0006811	biological_process	monoatomic ion transport
A	0006826	biological_process	iron ion transport
A	0006879	biological_process	intracellular iron ion homeostasis
A	0007166	biological_process	cell surface receptor signaling pathway
A	0008198	molecular_function	ferrous iron binding
A	0008199	molecular_function	ferric iron binding
A	0009617	biological_process	response to bacterium
A	0009925	cellular_component	basal plasma membrane
A	0009986	cellular_component	cell surface
A	0010008	cellular_component	endosome membrane
A	0016020	cellular_component	membrane
A	0016324	cellular_component	apical plasma membrane
A	0019731	biological_process	antibacterial humoral response
A	0019899	molecular_function	enzyme binding
A	0030139	cellular_component	endocytic vesicle
A	0030316	biological_process	osteoclast differentiation
A	0030669	cellular_component	clathrin-coated endocytic vesicle membrane
A	0031410	cellular_component	cytoplasmic vesicle
A	0031647	biological_process	regulation of protein stability
A	0031982	cellular_component	vesicle
A	0032436	biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process
A	0034774	cellular_component	secretory granule lumen
A	0034986	molecular_function	iron chaperone activity
A	0044325	molecular_function	transmembrane transporter binding
A	0045178	cellular_component	basal part of cell
A	0046872	molecular_function	metal ion binding
A	0048260	biological_process	positive regulation of receptor-mediated endocytosis
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0055037	cellular_component	recycling endosome
A	0060586	biological_process	multicellular organismal-level iron ion homeostasis
A	0070062	cellular_component	extracellular exosome
A	0071281	biological_process	cellular response to iron ion
A	0072562	cellular_component	blood microparticle
A	1903988	biological_process	iron ion export across plasma membrane
A	1990459	molecular_function	transferrin receptor binding
A	1990712	cellular_component	HFE-transferrin receptor complex
B	0005506	molecular_function	iron ion binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005768	cellular_component	endosome
B	0005769	cellular_component	early endosome
B	0005770	cellular_component	late endosome
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0005886	cellular_component	plasma membrane
B	0005905	cellular_component	clathrin-coated pit
B	0006811	biological_process	monoatomic ion transport
B	0006826	biological_process	iron ion transport
B	0006879	biological_process	intracellular iron ion homeostasis
B	0007166	biological_process	cell surface receptor signaling pathway
B	0008198	molecular_function	ferrous iron binding
B	0008199	molecular_function	ferric iron binding
B	0009617	biological_process	response to bacterium
B	0009925	cellular_component	basal plasma membrane
B	0009986	cellular_component	cell surface
B	0010008	cellular_component	endosome membrane
B	0016020	cellular_component	membrane
B	0016324	cellular_component	apical plasma membrane
B	0019731	biological_process	antibacterial humoral response
B	0019899	molecular_function	enzyme binding
B	0030139	cellular_component	endocytic vesicle
B	0030316	biological_process	osteoclast differentiation
B	0030669	cellular_component	clathrin-coated endocytic vesicle membrane
B	0031410	cellular_component	cytoplasmic vesicle
B	0031647	biological_process	regulation of protein stability
B	0031982	cellular_component	vesicle
B	0032436	biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process
B	0034774	cellular_component	secretory granule lumen
B	0034986	molecular_function	iron chaperone activity
B	0044325	molecular_function	transmembrane transporter binding
B	0045178	cellular_component	basal part of cell
B	0046872	molecular_function	metal ion binding
B	0048260	biological_process	positive regulation of receptor-mediated endocytosis
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0055037	cellular_component	recycling endosome
B	0060586	biological_process	multicellular organismal-level iron ion homeostasis
B	0070062	cellular_component	extracellular exosome
B	0071281	biological_process	cellular response to iron ion
B	0072562	cellular_component	blood microparticle
B	1903988	biological_process	iron ion export across plasma membrane
B	1990459	molecular_function	transferrin receptor binding
B	1990712	cellular_component	HFE-transferrin receptor complex

Functional Information from PROSITE/UniProt

site_id	PS00205
Number of Residues	10
Details	TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD

Chain	Residue	Details
A	TYR95-ASP104
A	TYR426-SER435

site_id	PS00206
Number of Residues	17
Details	TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF

Chain	Residue	Details
A	TYR188-PHE204
A	TYR517-PHE532

site_id	PS00207
Number of Residues	31
Details	TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV

Chain	Residue	Details
A	GLN222-VAL252
A	ASP558-VAL588

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	644
Details	Domain: {"description":"Transferrin-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	644
Details	Domain: {"description":"Transferrin-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V83","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Dimethylated arginine","evidences":[{"source":"UniProtKB","id":"P12346","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (GalNAc...) serine","featureId":"CAR_000073"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; atypical; partial","evidences":[{"source":"PubMed","id":"15536627","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)