Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6SOY

Trypanosoma brucei transferrin receptor in complex with human transferrin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0042783	biological_process	evasion of host immune response
B	0042783	biological_process	evasion of host immune response
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005768	cellular_component	endosome
C	0005769	cellular_component	early endosome
C	0005770	cellular_component	late endosome
C	0005788	cellular_component	endoplasmic reticulum lumen
C	0005886	cellular_component	plasma membrane
C	0005905	cellular_component	clathrin-coated pit
C	0006826	biological_process	iron ion transport
C	0006879	biological_process	intracellular iron ion homeostasis
C	0007015	biological_process	actin filament organization
C	0008198	molecular_function	ferrous iron binding
C	0008199	molecular_function	ferric iron binding
C	0009617	biological_process	response to bacterium
C	0009925	cellular_component	basal plasma membrane
C	0009986	cellular_component	cell surface
C	0010008	cellular_component	endosome membrane
C	0016020	cellular_component	membrane
C	0016324	cellular_component	apical plasma membrane
C	0019731	biological_process	antibacterial humoral response
C	0030139	cellular_component	endocytic vesicle
C	0030316	biological_process	osteoclast differentiation
C	0030669	cellular_component	clathrin-coated endocytic vesicle membrane
C	0031410	cellular_component	cytoplasmic vesicle
C	0031647	biological_process	regulation of protein stability
C	0031982	cellular_component	vesicle
C	0034756	biological_process	regulation of iron ion transport
C	0034774	cellular_component	secretory granule lumen
C	0034986	molecular_function	iron chaperone activity
C	0042327	biological_process	positive regulation of phosphorylation
C	0045178	cellular_component	basal part of cell
C	0045780	biological_process	positive regulation of bone resorption
C	0045893	biological_process	positive regulation of DNA-templated transcription
C	0046872	molecular_function	metal ion binding
C	0048260	biological_process	positive regulation of receptor-mediated endocytosis
C	0048471	cellular_component	perinuclear region of cytoplasm
C	0055037	cellular_component	recycling endosome
C	0070062	cellular_component	extracellular exosome
C	0070371	biological_process	ERK1 and ERK2 cascade
C	0071281	biological_process	cellular response to iron ion
C	0072562	cellular_component	blood microparticle
C	1990459	molecular_function	transferrin receptor binding
C	1990712	cellular_component	HFE-transferrin receptor complex
C	2000147	biological_process	positive regulation of cell motility

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	GLN222-VAL252
C	ASP558-VAL588

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

Chain	Residue	Details
C	TYR95-ASP104
C	TYR426-SER435

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

Chain	Residue	Details
C	TYR188-PHE204
C	TYR517-PHE532

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:22327295, ECO:0007744\|PDB:3V83

Chain	Residue	Details
C	ASP63
C	TYR95
C	TYR188
C	HIS249

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
C	THR120
C	ARG124
C	ALA126
C	GLY127

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00741, ECO:0000269\|PubMed:22327295, ECO:0000269\|PubMed:22343719, ECO:0000269\|PubMed:31636418, ECO:0007744\|PDB:3V83, ECO:0007744\|PDB:3VE1, ECO:0007744\|PDB:6SOY, ECO:0007744\|PDB:6SOZ

Chain	Residue	Details
C	TYR517
C	HIS585
C	ASP392
C	TYR426

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00741

Chain	Residue	Details
C	ALA458
C	GLY459
C	THR452
C	ARG456

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Dimethylated arginine => ECO:0000250\|UniProtKB:P12346

Chain	Residue	Details
C	ARG23

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269\|PubMed:26091039

Chain	Residue	Details
C	SER370
C	SER666

site_id	SWS_FT_FI7
Number of Residues	1
Details	CARBOHYD: O-linked (GalNAc...) serine

Chain	Residue	Details
C	SER32

site_id	SWS_FT_FI8
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269\|PubMed:14760718, ECO:0000269\|PubMed:15084671, ECO:0000269\|PubMed:15536627, ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:19838169, ECO:0000269\|PubMed:22327295, ECO:0000269\|PubMed:31636418, ECO:0007744\|PDB:6SOY, ECO:0007744\|PDB:6SOZ

Chain	Residue	Details
C	ASN413

site_id	SWS_FT_FI9
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; atypical; partial => ECO:0000269\|PubMed:15536627

Chain	Residue	Details
C	ASN472

site_id	SWS_FT_FI10
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269\|PubMed:14760718, ECO:0000269\|PubMed:15084671, ECO:0000269\|PubMed:15536627, ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:16740002, ECO:0000269\|PubMed:19139490, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:19838169, ECO:0000269\|PubMed:22327295

Chain	Residue	Details
C	ASN611

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