Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4EOH

Crystal Structure of Human PL Kinase with bound Theophylline

Replaces: 3KBI

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	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	0016740	molecular_function	transferase 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	0042822	biological_process	pyridoxal phosphate metabolic process
A	0046872	molecular_function	metal ion binding
A	0070062	cellular_component	extracellular exosome
B	0000166	molecular_function	nucleotide binding
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	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	0016740	molecular_function	transferase 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	0042822	biological_process	pyridoxal phosphate metabolic process
B	0046872	molecular_function	metal ion binding
B	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 401

Chain	Residue
A	GLU153
A	HOH536
A	HOH537
A	HOH538
A	HOH539
A	HOH645

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TEP A 402

Chain	Residue
A	ASP235
A	HOH546
A	HOH631
A	HOH633
A	SER12
A	GLY20
A	VAL231

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD A 403

Chain	Residue
A	SER12
A	PHE43
A	HIS46
A	THR47
A	HOH647

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MPD A 404

Chain	Residue
A	THR186
A	GLY234
A	LEU263

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD A 405

Chain	Residue
A	LYS76
A	TYR77
A	ASP78
A	ASN105
A	HOH636

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD A 406

Chain	Residue
A	ILE223
A	ARG224
A	VAL226
A	HIS264
A	HOH541

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MPD A 407

Chain	Residue
A	CYS5
A	LEU31
A	GLY32
A	LYS247

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 408

Chain	Residue
A	LEU156
A	LYS161

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 409

Chain	Residue
A	ARG70
A	MET93
A	GLU100

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 410

Chain	Residue
A	SER40
A	VAL56
A	THR85
A	ARG86
A	ASP87
A	PHE90
A	HOH600

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA B 401

Chain	Residue
B	GLU153
B	HOH615
B	HOH628
B	HOH690
B	HOH691

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TEP B 402

Chain	Residue
B	SER12
B	TYR84
B	VAL231
B	ASP235
B	HOH630
B	HOH660
B	HOH693

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MPD B 403

Chain	Residue
B	HIS46
B	THR47
B	TYR84
B	MPD407

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MPD B 404

Chain	Residue
B	ASP181
B	ARG208

site_id	BC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MPD B 405

Chain	Residue
B	PRO193

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MPD B 406

Chain	Residue
B	MET126
B	GLU130
B	LEU156
B	HOH636

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD B 407

Chain	Residue
A	SER192
A	PRO193
B	PHE43
B	TYR84
B	ARG86
B	MPD403

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MPD B 408

Chain	Residue
B	THR186
B	THR233

site_id	CC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MPD B 409

Chain	Residue
B	VAL109
B	THR245
B	PRO249
B	HOH514
B	HOH572
B	HOH678
B	HOH684

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD B 410

Chain	Residue
B	ILE223
B	ARG224
B	VAL226
B	HIS264
B	LEU267

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD B 411

Chain	Residue
B	ILE223
B	ARG224
B	HIS264
B	VAL306
B	VAL307

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 412

Chain	Residue
B	GLN63
B	GLU100
B	HOH689

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 413

Chain	Residue
B	CYS5
B	ASP78
B	HIS246
B	HOH581
B	HOH663
B	GLU4

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 414

Chain	Residue
B	CYS5
B	LEU31
B	GLY32
B	PHE33
B	HIS246
B	LYS247

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 415

Chain	Residue
B	GLU155
B	LEU156

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19351586","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19351586","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FHX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of PL kinase in complex with MgATP and PLP: Structural basis of severe induced MgATP substrate inhibition of the enzyme.","authors":["Gandhi A.K.","Musayev F.N.","Safo M.K."]}},{"source":"PDB","id":"3KEU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19351586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22879864","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EN4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17766369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19351586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22879864","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of PL kinase in complex with MgATP and PLP: Structural basis of severe induced MgATP substrate inhibition of the enzyme.","authors":["Gandhi A.K.","Musayev F.N.","Safo M.K."]}},{"source":"PDB","id":"3FHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KEU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EN4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17766369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19351586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22879864","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of PL kinase in complex with MgATP and PLP: Structural basis of severe induced MgATP substrate inhibition of the enzyme.","authors":["Gandhi A.K.","Musayev F.N.","Safo M.K."]}},{"source":"PDB","id":"2YXT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KEU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EN4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19351586","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of PL kinase in complex with MgATP and PLP: Structural basis of severe induced MgATP substrate inhibition of the enzyme.","authors":["Gandhi A.K.","Musayev F.N.","Safo M.K."]}},{"source":"PDB","id":"3FHY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KEU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17766369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19351586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22879864","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of PL kinase in complex with MgATP and PLP: Structural basis of severe induced MgATP substrate inhibition of the enzyme.","authors":["Gandhi A.K.","Musayev F.N.","Safo M.K."]}},{"source":"PDB","id":"2YXU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FHY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KEU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EN4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22879864","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of PL kinase in complex with MgATP and PLP: Structural basis of severe induced MgATP substrate inhibition of the enzyme.","authors":["Gandhi A.K.","Musayev F.N.","Safo M.K."]}},{"source":"PDB","id":"3KEU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EN4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19351586","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of PL kinase in complex with MgATP and PLP: Structural basis of severe induced MgATP substrate inhibition of the enzyme.","authors":["Gandhi A.K.","Musayev F.N.","Safo M.K."]}},{"source":"PDB","id":"3FHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KEU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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