Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1UOR

X-RAY STUDY OF RECOMBINANT HUMAN SERUM ALBUMIN. PHASES DETERMINED BY MOLECULAR REPLACEMENT METHOD, USING LOW RESOLUTION STRUCTURE MODEL OF TETRAGONAL FORM OF HUMAN SERUM ALBUMIN

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	0005783	cellular_component	endoplasmic reticulum
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005794	cellular_component	Golgi apparatus
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	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	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

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	192
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	197
Details	Domain: {"description":"Albumin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00769","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P02769","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
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	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"656055","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	37
Details	Site: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Site: {"description":"Aspirin-acetylated lysine"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
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	1
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	1
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	1
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	4
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	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07724","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	1
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	4
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	13
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	1
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	2
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	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Redhill","featureId":"CAR_000226"}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Casebrook","featureId":"CAR_000069"}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	1
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	1
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)