Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3BEX

Type III pantothenate kinase from Thermotoga maritima complexed with pantothenate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004594	molecular_function	pantothenate kinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0015937	biological_process	coenzyme A biosynthetic process
A	0016301	molecular_function	kinase activity
A	0043169	molecular_function	cation binding
A	0046872	molecular_function	metal ion binding
B	0004594	molecular_function	pantothenate kinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0015937	biological_process	coenzyme A biosynthetic process
B	0016301	molecular_function	kinase activity
B	0043169	molecular_function	cation binding
B	0046872	molecular_function	metal ion binding
C	0004594	molecular_function	pantothenate kinase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0015937	biological_process	coenzyme A biosynthetic process
C	0016301	molecular_function	kinase activity
C	0043169	molecular_function	cation binding
C	0046872	molecular_function	metal ion binding
D	0004594	molecular_function	pantothenate kinase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0015937	biological_process	coenzyme A biosynthetic process
D	0016301	molecular_function	kinase activity
D	0043169	molecular_function	cation binding
D	0046872	molecular_function	metal ion binding
E	0004594	molecular_function	pantothenate kinase activity
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0015937	biological_process	coenzyme A biosynthetic process
E	0016301	molecular_function	kinase activity
E	0043169	molecular_function	cation binding
E	0046872	molecular_function	metal ion binding
F	0004594	molecular_function	pantothenate kinase activity
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0015937	biological_process	coenzyme A biosynthetic process
F	0016301	molecular_function	kinase activity
F	0043169	molecular_function	cation binding
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 A 247

Chain	Residue
A	GLY8
A	HOH324
A	HOH540
A	ASN9
A	THR10
A	HIS11
A	THR128
A	HOH260
A	HOH276
A	HOH307
A	HOH314

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 B 247

Chain	Residue
B	GLY8
B	ASN9
B	THR10
B	HIS11
B	THR128
B	HOH257
B	HOH269
B	HOH278
B	HOH297
B	HOH308
B	HOH497

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 C 247

Chain	Residue
C	GLY8
C	ASN9
C	THR10
C	HIS11
C	THR128
C	HOH261
C	HOH265
C	HOH286
C	HOH288
C	HOH346
C	HOH360

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PO4 D 247

Chain	Residue
D	GLY8
D	ASN9
D	THR10
D	HIS11
D	THR128
D	HOH263
D	HOH291
D	HOH312
D	HOH319
D	HOH341
D	HOH393
D	HOH549

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 E 247

Chain	Residue
E	GLY8
E	ASN9
E	THR10
E	HIS11
E	THR128
E	HOH264
E	HOH292
E	HOH293
E	HOH295
E	HOH322
E	HOH434

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 F 247

Chain	Residue
F	GLY8
F	ASN9
F	THR10
F	HIS11
F	THR128
F	HOH265
F	HOH274
F	HOH288
F	HOH293
F	HOH325

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PAU A 248

Chain	Residue
A	GLU101
A	GLY103
A	ASP105
A	ARG106
A	THR131
A	HOH250
A	HOH260
A	HOH307
A	HOH340
B	LYS162
B	LEU163
B	THR179

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PAU B 248

Chain	Residue
A	LYS162
A	LEU163
A	THR179
B	GLU101
B	GLY103
B	ASP105
B	ARG106
B	HOH255
B	HOH308
B	HOH348

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PAU C 248

Chain	Residue
C	GLU101
C	GLY103
C	ASP105
C	ARG106
C	HOH249
C	HOH355
C	HOH360
D	LYS162
D	THR179

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PAU D 248

Chain	Residue
C	THR179
D	GLU101
D	GLY103
D	ASP105
D	ARG106
D	HOH251
D	HOH263
D	HOH319
D	HOH344
C	LYS162
C	LEU163

site_id	BC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PAU E 248

Chain	Residue
E	GLU101
E	GLY103
E	ASP105
E	ARG106
E	THR131
E	HOH256
E	HOH320
E	HOH322
F	LYS162
F	LEU163
F	THR179

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PAU F 248

Chain	Residue
E	LYS162
E	LEU163
E	THR179
F	GLU101
F	GLY103
F	ASP105
F	ARG106
F	HOH249
F	HOH265
F	HOH325
F	HOH332

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton acceptor => ECO:0000255

Chain	Residue	Details
A	ASP105
B	ASP105
C	ASP105
D	ASP105
E	ASP105
F	ASP105

site_id	SWS_FT_FI2
Number of Residues	18
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ASP6
D	ASP6
D	GLY103
D	THR179
E	ASP6
E	GLY103
E	THR179
F	ASP6
F	GLY103
F	THR179
A	GLY103
A	THR179
B	ASP6
B	GLY103
B	THR179
C	ASP6
C	GLY103
C	THR179

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255

Chain	Residue	Details
A	ASP125
E	THR128
F	ASP125
F	THR128
A	THR128
B	ASP125
B	THR128
C	ASP125
C	THR128
D	ASP125
D	THR128
E	ASP125

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