Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2A3Y

Pentameric crystal structure of human serum amyloid P-component bound to Bis-1,2-{[(Z)-2carboxy-2-methyl-1,3-dioxane]-5-yloxycarbamoyl}-ethane.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001849	molecular_function	complement component C1q complex binding
A	0002674	biological_process	negative regulation of acute inflammatory response
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0006457	biological_process	protein folding
A	0006953	biological_process	acute-phase response
A	0030246	molecular_function	carbohydrate binding
A	0042802	molecular_function	identical protein binding
A	0044871	biological_process	negative regulation by host of viral glycoprotein metabolic process
A	0045087	biological_process	innate immune response
A	0045656	biological_process	negative regulation of monocyte differentiation
A	0046597	biological_process	host-mediated suppression of symbiont invasion
A	0046790	molecular_function	virion binding
A	0046872	molecular_function	metal ion binding
A	0048525	biological_process	negative regulation of viral process
A	0051082	molecular_function	unfolded protein binding
A	0051131	biological_process	chaperone-mediated protein complex assembly
A	0061045	biological_process	negative regulation of wound healing
A	0070062	cellular_component	extracellular exosome
A	0072562	cellular_component	blood microparticle
A	1903019	biological_process	negative regulation of glycoprotein metabolic process
B	0001849	molecular_function	complement component C1q complex binding
B	0002674	biological_process	negative regulation of acute inflammatory response
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005634	cellular_component	nucleus
B	0006457	biological_process	protein folding
B	0006953	biological_process	acute-phase response
B	0030246	molecular_function	carbohydrate binding
B	0042802	molecular_function	identical protein binding
B	0044871	biological_process	negative regulation by host of viral glycoprotein metabolic process
B	0045087	biological_process	innate immune response
B	0045656	biological_process	negative regulation of monocyte differentiation
B	0046597	biological_process	host-mediated suppression of symbiont invasion
B	0046790	molecular_function	virion binding
B	0046872	molecular_function	metal ion binding
B	0048525	biological_process	negative regulation of viral process
B	0051082	molecular_function	unfolded protein binding
B	0051131	biological_process	chaperone-mediated protein complex assembly
B	0061045	biological_process	negative regulation of wound healing
B	0070062	cellular_component	extracellular exosome
B	0072562	cellular_component	blood microparticle
B	1903019	biological_process	negative regulation of glycoprotein metabolic process
C	0001849	molecular_function	complement component C1q complex binding
C	0002674	biological_process	negative regulation of acute inflammatory response
C	0005509	molecular_function	calcium ion binding
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005634	cellular_component	nucleus
C	0006457	biological_process	protein folding
C	0006953	biological_process	acute-phase response
C	0030246	molecular_function	carbohydrate binding
C	0042802	molecular_function	identical protein binding
C	0044871	biological_process	negative regulation by host of viral glycoprotein metabolic process
C	0045087	biological_process	innate immune response
C	0045656	biological_process	negative regulation of monocyte differentiation
C	0046597	biological_process	host-mediated suppression of symbiont invasion
C	0046790	molecular_function	virion binding
C	0046872	molecular_function	metal ion binding
C	0048525	biological_process	negative regulation of viral process
C	0051082	molecular_function	unfolded protein binding
C	0051131	biological_process	chaperone-mediated protein complex assembly
C	0061045	biological_process	negative regulation of wound healing
C	0070062	cellular_component	extracellular exosome
C	0072562	cellular_component	blood microparticle
C	1903019	biological_process	negative regulation of glycoprotein metabolic process
D	0001849	molecular_function	complement component C1q complex binding
D	0002674	biological_process	negative regulation of acute inflammatory response
D	0005509	molecular_function	calcium ion binding
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0005634	cellular_component	nucleus
D	0006457	biological_process	protein folding
D	0006953	biological_process	acute-phase response
D	0030246	molecular_function	carbohydrate binding
D	0042802	molecular_function	identical protein binding
D	0044871	biological_process	negative regulation by host of viral glycoprotein metabolic process
D	0045087	biological_process	innate immune response
D	0045656	biological_process	negative regulation of monocyte differentiation
D	0046597	biological_process	host-mediated suppression of symbiont invasion
D	0046790	molecular_function	virion binding
D	0046872	molecular_function	metal ion binding
D	0048525	biological_process	negative regulation of viral process
D	0051082	molecular_function	unfolded protein binding
D	0051131	biological_process	chaperone-mediated protein complex assembly
D	0061045	biological_process	negative regulation of wound healing
D	0070062	cellular_component	extracellular exosome
D	0072562	cellular_component	blood microparticle
D	1903019	biological_process	negative regulation of glycoprotein metabolic process
E	0001849	molecular_function	complement component C1q complex binding
E	0002674	biological_process	negative regulation of acute inflammatory response
E	0005509	molecular_function	calcium ion binding
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005615	cellular_component	extracellular space
E	0005634	cellular_component	nucleus
E	0006457	biological_process	protein folding
E	0006953	biological_process	acute-phase response
E	0030246	molecular_function	carbohydrate binding
E	0042802	molecular_function	identical protein binding
E	0044871	biological_process	negative regulation by host of viral glycoprotein metabolic process
E	0045087	biological_process	innate immune response
E	0045656	biological_process	negative regulation of monocyte differentiation
E	0046597	biological_process	host-mediated suppression of symbiont invasion
E	0046790	molecular_function	virion binding
E	0046872	molecular_function	metal ion binding
E	0048525	biological_process	negative regulation of viral process
E	0051082	molecular_function	unfolded protein binding
E	0051131	biological_process	chaperone-mediated protein complex assembly
E	0061045	biological_process	negative regulation of wound healing
E	0070062	cellular_component	extracellular exosome
E	0072562	cellular_component	blood microparticle
E	1903019	biological_process	negative regulation of glycoprotein metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 600

Chain	Residue
A	ASP58
A	ASN59
A	GLU136
A	GLN137
A	ASP138
A	CPJ610

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 601

Chain	Residue
A	CPJ610
A	HOH687
A	HOH688
A	GLU136
A	ASP138
A	GLN148

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 602

Chain	Residue
B	ASP58
B	ASN59
B	GLU136
B	GLN137
B	ASP138
B	CPJ611

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 603

Chain	Residue
B	GLU136
B	ASP138
B	GLN148
B	CPJ611
B	HOH656
B	HOH657

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 604

Chain	Residue
C	ASP58
C	ASN59
C	GLU136
C	GLN137
C	ASP138
C	CPJ612

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 605

Chain	Residue
C	GLU136
C	ASP138
C	GLN148
C	CPJ612
C	HOH709
C	HOH710

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 606

Chain	Residue
D	ASP58
D	ASN59
D	GLU136
D	GLN137
D	ASP138
D	CPJ614

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 607

Chain	Residue
D	GLU136
D	ASP138
D	GLN148
D	CPJ614
D	HOH752
D	HOH753

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 608

Chain	Residue
E	ASP58
E	ASN59
E	GLU136
E	GLN137
E	ASP138
E	CPJ613

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 609

Chain	Residue
E	GLU136
E	ASP138
E	GLN148
E	CPJ613
E	HOH707
E	HOH708

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CPJ A 610

Chain	Residue
A	ASP58
A	ASN59
A	GLU136
A	ASP138
A	GLN148
A	CA600
A	CA601

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CPJ B 611

Chain	Residue
B	ASP58
B	ASN59
B	TYR74
B	GLU136
B	ASP138
B	GLN148
B	CA602
B	CA603

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CPJ C 612

Chain	Residue
C	ASP58
C	ASN59
C	GLU136
C	ASP138
C	GLN148
C	CA604
C	CA605

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CPJ E 613

Chain	Residue
E	ASP58
E	ASN59
E	TYR64
E	GLU136
E	ASP138
E	GLN148
E	CA608
E	CA609

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CPJ D 614

Chain	Residue
D	ASP58
D	ASN59
D	GLU136
D	ASP138
D	GLN148
D	CA606
D	CA607
D	HOH756

Functional Information from PROSITE/UniProt

site_id	PS00289
Number of Residues	8
Details	PTX_1 Pentraxin domain signature. HiCvSWeS

Chain	Residue	Details
A	HIS93-SER100

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	995
Details	Domain: {"description":"Pentraxin (PTX)","evidences":[{"source":"PROSITE-ProRule","id":"PRU01172","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01172","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	5
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000169","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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