Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7AAI

Crystal structure of Human serum albumin in complex with perfluorooctanoic acid (PFOA) at 2.10 Angstrom Resolution

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
AAA	0003677	molecular_function	DNA binding
AAA	0005504	molecular_function	fatty acid binding
AAA	0005507	molecular_function	copper ion binding
AAA	0005515	molecular_function	protein binding
AAA	0005576	cellular_component	extracellular region
AAA	0005615	cellular_component	extracellular space
AAA	0005634	cellular_component	nucleus
AAA	0005737	cellular_component	cytoplasm
AAA	0005783	cellular_component	endoplasmic reticulum
AAA	0005788	cellular_component	endoplasmic reticulum lumen
AAA	0005794	cellular_component	Golgi apparatus
AAA	0008289	molecular_function	lipid binding
AAA	0009267	biological_process	cellular response to starvation
AAA	0015643	molecular_function	toxic substance binding
AAA	0016209	molecular_function	antioxidant activity
AAA	0019825	molecular_function	oxygen binding
AAA	0030170	molecular_function	pyridoxal phosphate binding
AAA	0031093	cellular_component	platelet alpha granule lumen
AAA	0031667	biological_process	response to nutrient levels
AAA	0032991	cellular_component	protein-containing complex
AAA	0042802	molecular_function	identical protein binding
AAA	0046872	molecular_function	metal ion binding
AAA	0051087	molecular_function	protein-folding chaperone binding
AAA	0051902	biological_process	negative regulation of mitochondrial depolarization
AAA	0070062	cellular_component	extracellular exosome
AAA	0072562	cellular_component	blood microparticle
AAA	0072732	biological_process	cellular response to calcium ion starvation
AAA	0098869	biological_process	cellular oxidant detoxification
AAA	0140272	molecular_function	exogenous protein binding
AAA	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
AAA	TYR161-LEU185
AAA	TYR353-PHE377
AAA	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	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P02770","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P02769","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
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_FI6
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"656055","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	37
Details	Site: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"15047055","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Site: {"description":"Aspirin-acetylated lysine"}

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"}]}

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":"18318008","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
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_FI12
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_FI13
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_FI14
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07724","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
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_FI19
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_FI20
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_FI21
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_FI22
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_FI23
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Redhill","featureId":"CAR_000226"}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant Casebrook","featureId":"CAR_000069"}

Chain

Residue

Details

site_id	SWS_FT_FI25
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_FI26
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)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)