Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8XMW

Local refinement of Hb-Hp bind to CD163

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
2	0004252	molecular_function	serine-type endopeptidase activity
2	0005576	cellular_component	extracellular region
2	0006508	biological_process	proteolysis
2	0030492	molecular_function	hemoglobin binding
A	0004601	molecular_function	peroxidase activity
A	0005344	molecular_function	oxygen carrier activity
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	0005829	cellular_component	cytosol
A	0005833	cellular_component	hemoglobin complex
A	0006954	biological_process	inflammatory response
A	0015670	biological_process	carbon dioxide transport
A	0015671	biological_process	oxygen transport
A	0016020	cellular_component	membrane
A	0019825	molecular_function	oxygen binding
A	0020037	molecular_function	heme binding
A	0030185	biological_process	nitric oxide transport
A	0031720	molecular_function	haptoglobin binding
A	0031838	cellular_component	haptoglobin-hemoglobin complex
A	0042542	biological_process	response to hydrogen peroxide
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0046872	molecular_function	metal ion binding
A	0048821	biological_process	erythrocyte development
A	0070062	cellular_component	extracellular exosome
A	0071682	cellular_component	endocytic vesicle lumen
A	0072562	cellular_component	blood microparticle
A	0098869	biological_process	cellular oxidant detoxification
B	0004601	molecular_function	peroxidase activity
B	0005344	molecular_function	oxygen carrier activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005829	cellular_component	cytosol
B	0005833	cellular_component	hemoglobin complex
B	0006954	biological_process	inflammatory response
B	0008217	biological_process	regulation of blood pressure
B	0015670	biological_process	carbon dioxide transport
B	0015671	biological_process	oxygen transport
B	0019825	molecular_function	oxygen binding
B	0020037	molecular_function	heme binding
B	0030185	biological_process	nitric oxide transport
B	0030492	molecular_function	hemoglobin binding
B	0031720	molecular_function	haptoglobin binding
B	0031721	molecular_function	hemoglobin alpha binding
B	0031838	cellular_component	haptoglobin-hemoglobin complex
B	0042542	biological_process	response to hydrogen peroxide
B	0042744	biological_process	hydrogen peroxide catabolic process
B	0045429	biological_process	positive regulation of nitric oxide biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0048821	biological_process	erythrocyte development
B	0070062	cellular_component	extracellular exosome
B	0070293	biological_process	renal absorption
B	0070527	biological_process	platelet aggregation
B	0071682	cellular_component	endocytic vesicle lumen
B	0072562	cellular_component	blood microparticle
B	0097746	biological_process	blood vessel diameter maintenance
B	0098869	biological_process	cellular oxidant detoxification
B	1904724	cellular_component	tertiary granule lumen
B	1904813	cellular_component	ficolin-1-rich granule lumen
D	0005044	molecular_function	scavenger receptor activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006953	biological_process	acute-phase response
D	0006954	biological_process	inflammatory response
D	0009897	cellular_component	external side of plasma membrane
D	0016020	cellular_component	membrane
D	0016192	biological_process	vesicle-mediated transport
D	0030666	cellular_component	endocytic vesicle membrane
D	0097110	molecular_function	scaffold protein binding
G	0005044	molecular_function	scavenger receptor activity
G	0005515	molecular_function	protein binding
G	0005576	cellular_component	extracellular region
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0005886	cellular_component	plasma membrane
G	0006953	biological_process	acute-phase response
G	0006954	biological_process	inflammatory response
G	0009897	cellular_component	external side of plasma membrane
G	0016020	cellular_component	membrane
G	0016192	biological_process	vesicle-mediated transport
G	0030666	cellular_component	endocytic vesicle membrane
G	0097110	molecular_function	scaffold protein binding

Functional Information from PROSITE/UniProt

site_id	PS00420
Number of Residues	38
Details	SRCR_1 SRCR domain signature. GenkcsGrvEvkvqeeWGtvCnngWsmeavsviCnqlG

Chain	Residue	Details
D	GLY56-GLY93
D	GLY271-GLY308
D	GLY724-GLY761
D	GLY934-GLY971

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	242
Details	Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	5
Details	Region: {"description":"Interaction with CD163","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	200
Details	Domain: {"description":"SRCR 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00196","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	200
Details	Domain: {"description":"SRCR 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00196","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	200
Details	Domain: {"description":"SRCR 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00196","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Site: {"description":"Cleavage; in calcium-free condition"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	8
Details	Peptide: {"description":"Hemopressin","featureId":"PRO_0000455882","evidences":[{"source":"PubMed","id":"18077343","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	140
Details	Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	1
Details	Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	32
Details	Site: {"description":"(Microbial infection) Cleavage; by N.americanus apr-2","evidences":[{"source":"PubMed","id":"12552433","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	8
Details	Site: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	5
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	3
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; alternate","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	5
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	9
Details	Peptide: {"description":"LVV-hemorphin-7","featureId":"PRO_0000296641"}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	6
Details	Peptide: {"description":"Spinorphin","featureId":"PRO_0000424226"}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	1
Details	Binding site: {"description":"distal binding residue"}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	1
Details	Binding site: {"description":"proximal binding residue"}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	1
Details	Modified residue: {"description":"N-pyruvate 2-iminyl-valine; in Hb A1b"}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"4531009","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	1
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"8637569","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9843411","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) valine; in Hb A1c","evidences":[{"source":"PubMed","id":"635569","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		Validation report (PDF)