Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4LKT

Crystal Structure of Human Epidermal Fatty Acid Binding Protein (FABP5) in Complex with Linoleic Acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001972	molecular_function	retinoic acid binding
A	0005324	molecular_function	long-chain fatty acid transmembrane transporter activity
A	0005504	molecular_function	fatty acid 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	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006006	biological_process	glucose metabolic process
A	0006629	biological_process	lipid metabolic process
A	0006656	biological_process	phosphatidylcholine biosynthetic process
A	0006869	biological_process	lipid transport
A	0008289	molecular_function	lipid binding
A	0008544	biological_process	epidermis development
A	0010829	biological_process	negative regulation of glucose transmembrane transport
A	0014069	cellular_component	postsynaptic density
A	0015908	biological_process	fatty acid transport
A	0015909	biological_process	long-chain fatty acid transport
A	0030667	cellular_component	secretory granule membrane
A	0031392	biological_process	regulation of prostaglandin biosynthetic process
A	0035360	biological_process	positive regulation of peroxisome proliferator activated receptor signaling pathway
A	0035578	cellular_component	azurophil granule lumen
A	0042593	biological_process	glucose homeostasis
A	0042802	molecular_function	identical protein binding
A	0045202	cellular_component	synapse
A	0051930	biological_process	regulation of sensory perception of pain
A	0070062	cellular_component	extracellular exosome
A	0099178	biological_process	regulation of retrograde trans-synaptic signaling by endocanabinoid
A	0120162	biological_process	positive regulation of cold-induced thermogenesis
A	1990379	biological_process	lipid transport across blood-brain barrier
B	0001972	molecular_function	retinoic acid binding
B	0005324	molecular_function	long-chain fatty acid transmembrane transporter activity
B	0005504	molecular_function	fatty acid 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	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006006	biological_process	glucose metabolic process
B	0006629	biological_process	lipid metabolic process
B	0006656	biological_process	phosphatidylcholine biosynthetic process
B	0006869	biological_process	lipid transport
B	0008289	molecular_function	lipid binding
B	0008544	biological_process	epidermis development
B	0010829	biological_process	negative regulation of glucose transmembrane transport
B	0014069	cellular_component	postsynaptic density
B	0015908	biological_process	fatty acid transport
B	0015909	biological_process	long-chain fatty acid transport
B	0030667	cellular_component	secretory granule membrane
B	0031392	biological_process	regulation of prostaglandin biosynthetic process
B	0035360	biological_process	positive regulation of peroxisome proliferator activated receptor signaling pathway
B	0035578	cellular_component	azurophil granule lumen
B	0042593	biological_process	glucose homeostasis
B	0042802	molecular_function	identical protein binding
B	0045202	cellular_component	synapse
B	0051930	biological_process	regulation of sensory perception of pain
B	0070062	cellular_component	extracellular exosome
B	0099178	biological_process	regulation of retrograde trans-synaptic signaling by endocanabinoid
B	0120162	biological_process	positive regulation of cold-induced thermogenesis
B	1990379	biological_process	lipid transport across blood-brain barrier
C	0001972	molecular_function	retinoic acid binding
C	0005324	molecular_function	long-chain fatty acid transmembrane transporter activity
C	0005504	molecular_function	fatty acid 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	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006006	biological_process	glucose metabolic process
C	0006629	biological_process	lipid metabolic process
C	0006656	biological_process	phosphatidylcholine biosynthetic process
C	0006869	biological_process	lipid transport
C	0008289	molecular_function	lipid binding
C	0008544	biological_process	epidermis development
C	0010829	biological_process	negative regulation of glucose transmembrane transport
C	0014069	cellular_component	postsynaptic density
C	0015908	biological_process	fatty acid transport
C	0015909	biological_process	long-chain fatty acid transport
C	0030667	cellular_component	secretory granule membrane
C	0031392	biological_process	regulation of prostaglandin biosynthetic process
C	0035360	biological_process	positive regulation of peroxisome proliferator activated receptor signaling pathway
C	0035578	cellular_component	azurophil granule lumen
C	0042593	biological_process	glucose homeostasis
C	0042802	molecular_function	identical protein binding
C	0045202	cellular_component	synapse
C	0051930	biological_process	regulation of sensory perception of pain
C	0070062	cellular_component	extracellular exosome
C	0099178	biological_process	regulation of retrograde trans-synaptic signaling by endocanabinoid
C	0120162	biological_process	positive regulation of cold-induced thermogenesis
C	1990379	biological_process	lipid transport across blood-brain barrier
D	0001972	molecular_function	retinoic acid binding
D	0005324	molecular_function	long-chain fatty acid transmembrane transporter activity
D	0005504	molecular_function	fatty acid 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	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006006	biological_process	glucose metabolic process
D	0006629	biological_process	lipid metabolic process
D	0006656	biological_process	phosphatidylcholine biosynthetic process
D	0006869	biological_process	lipid transport
D	0008289	molecular_function	lipid binding
D	0008544	biological_process	epidermis development
D	0010829	biological_process	negative regulation of glucose transmembrane transport
D	0014069	cellular_component	postsynaptic density
D	0015908	biological_process	fatty acid transport
D	0015909	biological_process	long-chain fatty acid transport
D	0030667	cellular_component	secretory granule membrane
D	0031392	biological_process	regulation of prostaglandin biosynthetic process
D	0035360	biological_process	positive regulation of peroxisome proliferator activated receptor signaling pathway
D	0035578	cellular_component	azurophil granule lumen
D	0042593	biological_process	glucose homeostasis
D	0042802	molecular_function	identical protein binding
D	0045202	cellular_component	synapse
D	0051930	biological_process	regulation of sensory perception of pain
D	0070062	cellular_component	extracellular exosome
D	0099178	biological_process	regulation of retrograde trans-synaptic signaling by endocanabinoid
D	0120162	biological_process	positive regulation of cold-induced thermogenesis
D	1990379	biological_process	lipid transport across blood-brain barrier

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EIC A 601

Chain	Residue
A	MET23
A	LEU60
A	ARG109
A	ARG129
A	TYR131
A	HOH720

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 602

Chain	Residue
A	ILE30
A	ARG33

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 603

Chain	Residue
A	SER66
A	GLU74
A	THR76
A	PHE65

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 604

Chain	Residue
A	ALA39
A	LYS40
A	SER58
A	THR59
C	LYS34
D	THR59

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 605

Chain	Residue
A	THR63
A	GLU75
A	THR76
A	THR77
A	GLN96
A	ARG109

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 606

Chain	Residue
A	SER16
A	LYS17
A	GLY18
A	PHE19
A	ASP20
A	GLU21

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EIC B 601

Chain	Residue
A	MET35
B	MET23
B	LEU26
B	LYS61
B	ASP79
B	ARG109
B	ARG129
B	TYR131
B	HOH706

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL B 602

Chain	Residue
B	LYS40
B	THR59

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 603

Chain	Residue
B	GLU75
B	THR77
B	ALA78
B	GLN96
B	GLN98
B	ARG109

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE TAR B 604

Chain	Residue
B	LYS24
B	ILE30
B	ILE30
B	ARG33
B	ARG33
B	HOH709

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EIC C 601

Chain	Residue
C	LEU32
C	GLY36
C	PRO41
C	ALA78
C	ASP79
C	CYS120
C	ARG129
C	TYR131
C	HOH718

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CIT C 602

Chain	Residue
B	ARG10
B	ARG12
C	SER58
C	THR59
C	LEU60
C	LYS61
C	THR62

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 603

Chain	Residue
C	HOH703
C	HOH706
D	GOL603

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 604

Chain	Residue
C	ILE30
C	ARG33

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NH4 C 605

Chain	Residue
C	GLY18
C	SO4606

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 606

Chain	Residue
C	SER16
C	LYS17
C	GLY18
C	PHE19
C	ASP20
C	NH4605

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE TAR C 607

Chain	Residue
B	GLY9
B	ARG10
B	LYS133
C	ARG10
C	LYS55
C	GLU57

site_id	BC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EIC D 601

Chain	Residue
D	LEU32
D	GLY36
D	ASP79
D	VAL118
D	CYS120
D	ARG129
D	TYR131
D	HOH708
D	HOH720

site_id	CC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 602

Chain	Residue
A	VAL134
D	SER58
D	THR59
D	LYS61
D	THR62
A	ARG10
A	ARG12

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 603

Chain	Residue
C	LYS61
C	GOL603
D	GLY29
D	ILE30
D	ARG33

site_id	CC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NH4 D 604

Chain	Residue
D	GLY18
D	SO4606

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NH4 D 605

Chain	Residue
D	SER16
D	ALA37
D	LYS40
D	ARG129
D	SO4606

site_id	CC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 606

Chain	Residue
D	SER16
D	LYS17
D	GLY18
D	PHE19
D	ASP20
D	NH4604
D	NH4605

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE TAR D 607

Chain	Residue
A	GLY9
A	LYS133
D	ARG10
D	LYS55
D	GLU57

Functional Information from PROSITE/UniProt

site_id	PS00214
Number of Residues	18
Details	FABP Cytosolic fatty-acid binding proteins signature. GRWrLvdSkGFDeYMKEL

Chain	Residue	Details
A	GLY9-LEU26

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:24531463, ECO:0007744\|PDB:4AZR

Chain	Residue	Details
A	CYS43
D	CYS43
D	ARG109
D	TYR131
A	ARG109
A	TYR131
B	CYS43
B	ARG109
B	TYR131
C	CYS43
C	ARG109
C	TYR131

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:24692551, ECO:0007744\|PDB:4LKT

Chain	Residue	Details
A	ARG129
B	ARG129
C	ARG129
D	ARG129

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: N-acetylalanine => ECO:0000269\|PubMed:12665801, ECO:0007744\|PubMed:19413330, ECO:0007744\|PubMed:22223895, ECO:0007744\|PubMed:22814378, ECO:0007744\|PubMed:25944712

Chain	Residue	Details
A	ALA2
B	ALA2
C	ALA2
D	ALA2

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS17
B	LYS17
C	LYS17
D	LYS17

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:15592455

Chain	Residue	Details
A	TYR131
B	TYR131
C	TYR131
D	TYR131

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