Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8WR2

Crystal Structure of Human Pyridoxal Kinase with bound Luteolin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005524	molecular_function	ATP binding
A	0005576	cellular_component	extracellular region
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008270	molecular_function	zinc ion binding
A	0008478	molecular_function	pyridoxal kinase activity
A	0009443	biological_process	pyridoxal 5'-phosphate salvage
A	0016301	molecular_function	kinase activity
A	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
A	0030170	molecular_function	pyridoxal phosphate binding
A	0030955	molecular_function	potassium ion binding
A	0031402	molecular_function	sodium ion binding
A	0031403	molecular_function	lithium ion binding
A	0034774	cellular_component	secretory granule lumen
A	0035580	cellular_component	specific granule lumen
A	0042803	molecular_function	protein homodimerization activity
A	0042816	biological_process	vitamin B6 metabolic process
A	0042817	biological_process	pyridoxal metabolic process
A	0042818	biological_process	pyridoxamine metabolic process
A	0042822	biological_process	pyridoxal phosphate metabolic process
A	0046872	molecular_function	metal ion binding
A	0070062	cellular_component	extracellular exosome
B	0000287	molecular_function	magnesium ion binding
B	0005524	molecular_function	ATP binding
B	0005576	cellular_component	extracellular region
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008270	molecular_function	zinc ion binding
B	0008478	molecular_function	pyridoxal kinase activity
B	0009443	biological_process	pyridoxal 5'-phosphate salvage
B	0016301	molecular_function	kinase activity
B	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
B	0030170	molecular_function	pyridoxal phosphate binding
B	0030955	molecular_function	potassium ion binding
B	0031402	molecular_function	sodium ion binding
B	0031403	molecular_function	lithium ion binding
B	0034774	cellular_component	secretory granule lumen
B	0035580	cellular_component	specific granule lumen
B	0042803	molecular_function	protein homodimerization activity
B	0042816	biological_process	vitamin B6 metabolic process
B	0042817	biological_process	pyridoxal metabolic process
B	0042818	biological_process	pyridoxamine metabolic process
B	0042822	biological_process	pyridoxal phosphate metabolic process
B	0046872	molecular_function	metal ion binding
B	0070062	cellular_component	extracellular exosome

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000305\|PubMed:19351586

Chain	Residue	Details
B	ASP235
A	ASP235

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:19351586, ECO:0007744\|PDB:3FHX

Chain	Residue	Details
B	SER12
A	SER12

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|Ref.16, ECO:0007744\|PDB:3KEU

Chain	Residue	Details
B	THR47
A	THR47

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:19351586, ECO:0000269\|PubMed:22879864, ECO:0007744\|PDB:3FHX, ECO:0007744\|PDB:4EN4

Chain	Residue	Details
B	ASP113
A	ASP113

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:17766369, ECO:0000269\|PubMed:19351586, ECO:0000269\|PubMed:22879864, ECO:0000269\|Ref.16, ECO:0007744\|PDB:3FHX, ECO:0007744\|PDB:3KEU, ECO:0007744\|PDB:4EN4

Chain	Residue	Details
B	ASP118
A	ASP118

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:17766369, ECO:0000269\|PubMed:19351586, ECO:0000269\|PubMed:22879864, ECO:0000269\|Ref.16, ECO:0007744\|PDB:2YXT, ECO:0007744\|PDB:3FHX, ECO:0007744\|PDB:3KEU, ECO:0007744\|PDB:4EN4

Chain	Residue	Details
B	THR148
B	THR186
A	THR148
A	THR186

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:19351586, ECO:0000269\|Ref.16, ECO:0007744\|PDB:3FHY, ECO:0007744\|PDB:3KEU

Chain	Residue	Details
B	ASN150
A	ASN150

site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:22879864, ECO:0000269\|Ref.16, ECO:0007744\|PDB:3KEU, ECO:0007744\|PDB:4EN4

Chain	Residue	Details
B	VAL226
A	VAL226

site_id	SWS_FT_FI9
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:17766369, ECO:0000269\|PubMed:19351586, ECO:0000269\|PubMed:22879864, ECO:0000269\|Ref.16, ECO:0007744\|PDB:2YXU, ECO:0007744\|PDB:3FHX, ECO:0007744\|PDB:3FHY, ECO:0007744\|PDB:3KEU, ECO:0007744\|PDB:4EN4

Chain	Residue	Details
B	THR233
A	THR233

site_id	SWS_FT_FI10
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:19351586, ECO:0000269\|Ref.16, ECO:0007744\|PDB:3FHX, ECO:0007744\|PDB:3KEU

Chain	Residue	Details
B	GLY234
A	GLY234

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: N-acetylmethionine => ECO:0000250\|UniProtKB:P82197

Chain	Residue	Details
B	MET1
A	MET1

site_id	SWS_FT_FI12
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19369195

Chain	Residue	Details
B	SER59
B	SER164
A	SER59
A	SER164

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18691976, ECO:0007744\|PubMed:19369195

Chain	Residue	Details
B	SER213
A	SER213

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18691976, ECO:0007744\|PubMed:19369195, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
B	SER285
A	SER285

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