Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3A73

Crystal Structure Analysis of Human serum albumin complexed with delta 12-prostaglandin J2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0005504	molecular_function	fatty acid binding
A	0005507	molecular_function	copper 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	0005737	cellular_component	cytoplasm
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0006783	biological_process	heme biosynthetic process
A	0008289	molecular_function	lipid binding
A	0009267	biological_process	cellular response to starvation
A	0015643	molecular_function	toxic substance binding
A	0015723	biological_process	bilirubin transport
A	0016209	molecular_function	antioxidant activity
A	0019825	molecular_function	oxygen binding
A	0020037	molecular_function	heme binding
A	0030170	molecular_function	pyridoxal phosphate binding
A	0031093	cellular_component	platelet alpha granule lumen
A	0031667	biological_process	response to nutrient levels
A	0032991	cellular_component	protein-containing complex
A	0034599	biological_process	cellular response to oxidative stress
A	0042167	biological_process	heme catabolic process
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0051087	molecular_function	protein-folding chaperone binding
A	0051902	biological_process	negative regulation of mitochondrial depolarization
A	0070062	cellular_component	extracellular exosome
A	0072562	cellular_component	blood microparticle
A	0072732	biological_process	cellular response to calcium ion starvation
A	0098869	biological_process	cellular oxidant detoxification
A	0140104	molecular_function	molecular carrier activity
A	0140272	molecular_function	exogenous protein binding
A	1903981	molecular_function	enterobactin binding
B	0003677	molecular_function	DNA binding
B	0005504	molecular_function	fatty acid binding
B	0005507	molecular_function	copper 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	0005737	cellular_component	cytoplasm
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0006783	biological_process	heme biosynthetic process
B	0008289	molecular_function	lipid binding
B	0009267	biological_process	cellular response to starvation
B	0015643	molecular_function	toxic substance binding
B	0015723	biological_process	bilirubin transport
B	0016209	molecular_function	antioxidant activity
B	0019825	molecular_function	oxygen binding
B	0020037	molecular_function	heme binding
B	0030170	molecular_function	pyridoxal phosphate binding
B	0031093	cellular_component	platelet alpha granule lumen
B	0031667	biological_process	response to nutrient levels
B	0032991	cellular_component	protein-containing complex
B	0034599	biological_process	cellular response to oxidative stress
B	0042167	biological_process	heme catabolic process
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0051087	molecular_function	protein-folding chaperone binding
B	0051902	biological_process	negative regulation of mitochondrial depolarization
B	0070062	cellular_component	extracellular exosome
B	0072562	cellular_component	blood microparticle
B	0072732	biological_process	cellular response to calcium ion starvation
B	0098869	biological_process	cellular oxidant detoxification
B	0140104	molecular_function	molecular carrier activity
B	0140272	molecular_function	exogenous protein binding
B	1903981	molecular_function	enterobactin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MYR A 1002

Chain	Residue
A	LEU14
A	HOH688
A	ALA26
A	PHE70
A	TYR150
A	LEU250
A	LEU251
A	ALA254
A	ARG257
A	SER287

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MYR A 1003

Chain	Residue
A	SER342
A	VAL344
A	ARG348
A	CYS392
A	ARG485

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MYR A 1004

Chain	Residue
A	TYR411
A	VAL415
A	VAL418
A	LEU453
A	LEU460
A	PHE488
A	SER489

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MYR A 1005

Chain	Residue
A	TYR401
A	ASN405
A	PHE507
A	LYS525
A	MET548
A	PHE551
A	ALA552
A	SER579

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MYR A 1006

Chain	Residue
A	VAL216
A	ASP324
A	GLY328
A	LYS351

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MYR A 1007

Chain	Residue
A	ARG222
A	ILE290

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PJ2 A 1011

Chain	Residue
A	MET123
A	PHE134
A	LEU135
A	TYR138
A	LEU139
A	ILE142
A	ALA158
A	TYR161
A	PHE165
A	PJ21012

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PJ2 A 1012

Chain	Residue
A	ARG114
A	LEU115
A	HIS146
A	PJ21011

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MYR B 1002

Chain	Residue
B	VAL23
B	LEU66
B	TYR150
B	PRO152
B	LEU251
B	ALA254
B	ARG257
B	ALA258
B	SER287

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MYR B 1003

Chain	Residue
B	SER342
B	VAL344
B	ARG348
B	ASN391
B	VAL433
B	LEU453
B	ARG485

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MYR B 1004

Chain	Residue
B	TYR411
B	VAL418
B	LEU460
B	SER489

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MYR B 1005

Chain	Residue
B	TYR401
B	PHE507
B	LYS525
B	LEU532
B	MET548
B	PHE551
B	ALA552
B	SER579

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MYR B 1006

Chain	Residue
B	ALA210
B	LYS212
B	VAL216
B	LEU347
B	LEU481
B	VAL482

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MYR B 1007

Chain	Residue
B	ARG222
B	LEU260
B	ALA291

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PJ2 B 1011

Chain	Residue
B	ARG117
B	MET123
B	TYR138
B	ILE142
B	ALA158
B	TYR161
B	PHE165

Functional Information from PROSITE/UniProt

site_id	PS00212
Number of Residues	25
Details	ALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL

Chain	Residue	Details
A	TYR161-LEU185
A	TYR353-PHE377
A	PHE551-LEU575

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	384
Details	Domain: {"description":"Albumin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00769","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P02770","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P02769","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"28567254","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IJF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"656055","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	70
Details	Site: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Site: {"description":"Aspirin-acetylated lysine"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
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	Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18318008","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	6
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P07724","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07724","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	26
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6853480","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Redhill","featureId":"CAR_000226"}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Casebrook","featureId":"CAR_000069"}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6706980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6853480","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; alternate","evidences":[{"source":"PubMed","id":"3759977","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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