Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6YK1

Crystal structure of mouse pyridoxal kinase in complex with ATP-gamma-S and artesunate

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	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	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	0070280	molecular_function	pyridoxal binding
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0005524	molecular_function	ATP binding
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	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	0070280	molecular_function	pyridoxal binding
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0005524	molecular_function	ATP binding
C	0005654	cellular_component	nucleoplasm
C	0005829	cellular_component	cytosol
C	0008270	molecular_function	zinc ion binding
C	0008478	molecular_function	pyridoxal kinase activity
C	0009443	biological_process	pyridoxal 5'-phosphate salvage
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
C	0030170	molecular_function	pyridoxal phosphate binding
C	0030955	molecular_function	potassium ion binding
C	0031402	molecular_function	sodium ion binding
C	0031403	molecular_function	lithium ion binding
C	0042803	molecular_function	protein homodimerization activity
C	0042816	biological_process	vitamin B6 metabolic process
C	0042822	biological_process	pyridoxal phosphate metabolic process
C	0046872	molecular_function	metal ion binding
C	0070280	molecular_function	pyridoxal binding
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0005524	molecular_function	ATP binding
D	0005654	cellular_component	nucleoplasm
D	0005829	cellular_component	cytosol
D	0008270	molecular_function	zinc ion binding
D	0008478	molecular_function	pyridoxal kinase activity
D	0009443	biological_process	pyridoxal 5'-phosphate salvage
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
D	0030170	molecular_function	pyridoxal phosphate binding
D	0030955	molecular_function	potassium ion binding
D	0031402	molecular_function	sodium ion binding
D	0031403	molecular_function	lithium ion binding
D	0042803	molecular_function	protein homodimerization activity
D	0042816	biological_process	vitamin B6 metabolic process
D	0042822	biological_process	pyridoxal phosphate metabolic process
D	0046872	molecular_function	metal ion binding
D	0070280	molecular_function	pyridoxal binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	binding site for residue GOL A 501

Chain	Residue
A	PRO191

site_id	AC2
Number of Residues	2
Details	binding site for residue PG4 A 502

Chain	Residue
A	GLY159
A	EDO505

site_id	AC3
Number of Residues	6
Details	binding site for residue D95 A 503

Chain	Residue
A	PHE43
A	THR47
A	TYR84
A	ARG86
A	ASP87
A	EDO512

site_id	AC4
Number of Residues	13
Details	binding site for residue AGS A 504

Chain	Residue
A	ASP113
A	ASP118
A	THR148
A	ASN150
A	GLU153
A	THR186
A	SER187
A	MET223
A	VAL226
A	ALA228
A	THR233
A	GLY234
A	LEU267

site_id	AC5
Number of Residues	1
Details	binding site for residue EDO A 505

Chain	Residue
A	PG4502

site_id	AC6
Number of Residues	7
Details	binding site for residue EDO A 506

Chain	Residue
A	ASN75
A	LYS76
A	TYR77
A	LEU101
A	GLN104
A	ASN105
A	EDO513

site_id	AC7
Number of Residues	7
Details	binding site for residue EDO A 507

Chain	Residue
A	GLN11
A	LEU81
A	THR82
A	GLY83
A	ASP113
A	ASP235
A	ALA238

site_id	AC8
Number of Residues	4
Details	binding site for residue EDO A 508

Chain	Residue
A	HIS46
A	THR47
A	VAL231
A	HOH603

site_id	AC9
Number of Residues	2
Details	binding site for residue EDO A 509

Chain	Residue
A	LYS119
A	GLY124

site_id	AD1
Number of Residues	4
Details	binding site for residue EDO A 510

Chain	Residue
A	HIS63
A	GLU67
A	MET93
A	GLU100

site_id	AD2
Number of Residues	2
Details	binding site for residue EDO A 511

Chain	Residue
A	VAL30
B	LYS297

site_id	AD3
Number of Residues	4
Details	binding site for residue EDO A 512

Chain	Residue
A	TRP52
A	GLY54
A	D95503
B	VAL306

site_id	AD4
Number of Residues	3
Details	binding site for residue EDO A 513

Chain	Residue
A	TYR77
A	ASP78
A	EDO506

site_id	AD5
Number of Residues	4
Details	binding site for residue EDO A 514

Chain	Residue
A	CYS5
A	LEU31
A	GLY32
A	LYS247

site_id	AD6
Number of Residues	1
Details	binding site for residue EDO A 515

Chain	Residue
A	THR182

site_id	AD7
Number of Residues	5
Details	binding site for residue GOL B 402

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

site_id	AD8
Number of Residues	15
Details	binding site for residue AGS B 403

Chain	Residue
B	ASP113
B	ASP118
B	THR148
B	ASN150
B	GLU153
B	THR186
B	SER187
B	MET223
B	ARG224
B	VAL226
B	ALA228
B	THR233
B	GLY234
B	LEU267
B	HOH514

site_id	AD9
Number of Residues	5
Details	binding site for residue EDO B 404

Chain	Residue
A	ASN72
B	ALA50
B	SER285
B	PRO286
B	ALA287

site_id	AE1
Number of Residues	3
Details	binding site for residue EDO B 405

Chain	Residue
B	SER12
B	THR47
B	EDO406

site_id	AE2
Number of Residues	3
Details	binding site for residue EDO B 406

Chain	Residue
B	PHE43
B	TYR84
B	EDO405

site_id	AE3
Number of Residues	4
Details	binding site for residue EDO B 407

Chain	Residue
A	ASN39
A	GLN42
B	ASN39
B	GLN42

site_id	AE4
Number of Residues	4
Details	binding site for residue EDO B 408

Chain	Residue
B	GLU100
B	HIS63
B	MET93
B	ASP96

site_id	AE5
Number of Residues	3
Details	binding site for residue EDO C 501

Chain	Residue
C	GLN104
C	SER106
C	ARG107

site_id	AE6
Number of Residues	2
Details	binding site for residue GOL C 503

Chain	Residue
C	THR47
C	HOH605

site_id	AE7
Number of Residues	5
Details	binding site for residue GOL C 504

Chain	Residue
C	LYS102
C	PRO142
C	ALA144
C	ASP145
C	GLY179

site_id	AE8
Number of Residues	15
Details	binding site for residue AGS C 505

Chain	Residue
C	ASP113
C	GLY117
C	ASP118
C	ASN150
C	GLU153
C	THR186
C	SER187
C	ARG224
C	VAL226
C	ALA228
C	THR233
C	GLY234
C	MET263
C	LEU267
C	HOH614

site_id	AE9
Number of Residues	2
Details	binding site for residue EDO C 506

Chain	Residue
C	HIS51
C	TRP52

site_id	AF1
Number of Residues	1
Details	binding site for residue EDO C 507

Chain	Residue
C	GLU166

site_id	AF2
Number of Residues	3
Details	binding site for residue EDO C 508

Chain	Residue
C	CYS5
C	LEU31
C	LYS247

site_id	AF3
Number of Residues	6
Details	binding site for residue EDO C 509

Chain	Residue
C	SER40
C	VAL56
C	LEU57
C	THR85
C	ARG86
C	PHE90

site_id	AF4
Number of Residues	5
Details	binding site for residue EDO C 510

Chain	Residue
C	LYS76
C	TYR77
C	LEU101
C	GLN104
C	ASN105

site_id	AF5
Number of Residues	3
Details	binding site for residue EDO C 511

Chain	Residue
C	HIS63
C	MET93
C	GLU100

site_id	AF6
Number of Residues	4
Details	binding site for residue EDO D 401

Chain	Residue
C	ASN39
C	GLN42
D	ASN39
D	GLN42

site_id	AF7
Number of Residues	16
Details	binding site for residue AGS D 402

Chain	Residue
D	ASP113
D	VAL115
D	ASP118
D	TYR127
D	THR148
D	ASN150
D	GLU153
D	THR186
D	SER187
D	VAL226
D	ALA228
D	THR233
D	GLY234
D	PHE237
D	MET263
D	LEU267

site_id	AF8
Number of Residues	3
Details	binding site for residue EDO D 403

Chain	Residue
D	LEU31
D	GLY32
D	PHE33

site_id	AF9
Number of Residues	3
Details	binding site for residue EDO D 404

Chain	Residue
D	PHE43
D	HIS46
D	THR47

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"O00764","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	56
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O00764","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O00764","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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