Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1E7H

HUMAN SERUM ALBUMIN COMPLEXED WITH HEXADECANOIC ACID (PALMITIC ACID)

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	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	0032991	cellular_component	protein-containing complex
A	0036094	molecular_function	small molecule binding
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	0140272	molecular_function	exogenous protein binding
A	1903981	molecular_function	enterobactin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PLM A1001

Chain	Residue
A	ARG117
A	LEU135
A	TYR138
A	TYR161
A	HOH2005

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PLM A1002

Chain	Residue
A	ALA254
A	ARG257
A	LEU283
A	SER287
A	VAL46
A	LEU69
A	TYR150
A	LEU251

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PLM A1003

Chain	Residue
A	SER342
A	VAL344
A	ARG348
A	ASN391
A	GLY434
A	LEU453
A	ARG485
A	PLM1004

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PLM A1004

Chain	Residue
A	LEU387
A	TYR411
A	LEU457
A	LEU460
A	LEU463
A	HIS464
A	SER489
A	PLM1003
A	HOH2016
A	HOH2028
A	HOH2029

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PLM A1005

Chain	Residue
A	TYR401
A	PHE502
A	PHE507
A	LYS525
A	ALA528
A	HIS535
A	MET548
A	GLN580

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PLM A1006

Chain	Residue
A	ARG209
A	ALA210
A	LYS351

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PLM A1007

Chain	Residue
A	ARG218
A	ARG222

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	1
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P02770

Chain	Residue	Details
A	HIS3

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P02769

Chain	Residue	Details
A	GLU6
A	ASP13
A	GLU244
A	GLU252
A	ASP255
A	ASP259

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:28567254, ECO:0007744\|PDB:5IJF

Chain	Residue	Details
A	HIS67
A	HIS247
A	ASP249

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:656055

Chain	Residue	Details
A	LYS240

site_id	SWS_FT_FI5
Number of Residues	37
Details	SITE: Not glycated => ECO:0000269\|PubMed:15047055

Chain	Residue	Details
A	LYS4
A	LYS174
A	LYS181
A	LYS190
A	LYS195
A	LYS205
A	LYS212
A	LYS240
A	LYS262
A	LYS274
A	LYS286
A	LYS20
A	LYS359
A	LYS372
A	LYS389
A	LYS402
A	LYS414
A	LYS432
A	LYS436
A	LYS466
A	LYS475
A	LYS500
A	LYS41
A	LYS519
A	LYS524
A	LYS538
A	LYS541
A	LYS557
A	LYS560
A	LYS564
A	LYS574
A	LYS64
A	LYS73
A	LYS93
A	LYS106
A	LYS136
A	LYS159

site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Aspirin-acetylated lysine

Chain	Residue	Details
A	LYS199

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269\|PubMed:26091039

Chain	Residue	Details
A	SER5

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269\|PubMed:26091039, ECO:0007744\|PubMed:18318008, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER58

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269\|PubMed:26091039, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER65

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by FAM20C => ECO:0000269\|PubMed:26091039

Chain	Residue	Details
A	THR83

site_id	SWS_FT_FI11
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P07724

Chain	Residue	Details
A	LYS205
A	LYS436
A	LYS519
A	LYS564

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P07724

Chain	Residue	Details
A	SER273

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19690332

Chain	Residue	Details
A	SER419

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:19690332

Chain	Residue	Details
A	THR420
A	THR422

site_id	SWS_FT_FI15
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER489

site_id	SWS_FT_FI16
Number of Residues	1
Details	MOD_RES: N6-methyllysine; alternate => ECO:0007744\|PubMed:24129315

Chain	Residue	Details
A	LYS534

site_id	SWS_FT_FI17
Number of Residues	4
Details	CARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:3759977

Chain	Residue	Details
A	LYS12
A	LYS281
A	LYS317
A	LYS439

site_id	SWS_FT_FI18
Number of Residues	13
Details	CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269\|PubMed:15047055

Chain	Residue	Details
A	LYS51
A	LYS444
A	LYS536
A	LYS545
A	LYS573
A	LYS137
A	LYS162
A	LYS225
A	LYS276
A	LYS313
A	LYS323
A	LYS378
A	LYS413

site_id	SWS_FT_FI19
Number of Residues	1
Details	CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269\|PubMed:3759977, ECO:0000269\|PubMed:6853480

Chain	Residue	Details
A	LYS199

site_id	SWS_FT_FI20
Number of Residues	2
Details	CARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:15047055, ECO:0000269\|PubMed:3759977

Chain	Residue	Details
A	LYS233
A	LYS351

site_id	SWS_FT_FI21
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; in variant Redhill

Chain	Residue	Details
A	ASN318

site_id	SWS_FT_FI22
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; in variant Casebrook

Chain	Residue	Details
A	ASP494

site_id	SWS_FT_FI23
Number of Residues	1
Details	CARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269\|PubMed:15047055, ECO:0000269\|PubMed:3759977, ECO:0000269\|PubMed:6706980, ECO:0000269\|PubMed:6853480

Chain	Residue	Details
A	LYS525

site_id	SWS_FT_FI24
Number of Residues	1
Details	CARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269\|PubMed:3759977

Chain	Residue	Details
A	LYS534

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