Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1GLF

CRYSTAL STRUCTURES OF ESCHERICHIA COLI GLYCEROL KINASE AND THE MUTANT A65T IN AN INACTIVE TETRAMER: CONFORMATIONAL CHANGES AND IMPLICATIONS FOR ALLOSTERIC REGULATION

Functional Information from GO Data

Chain	GOid	namespace	contents
O	0004370	molecular_function	glycerol kinase activity
O	0005515	molecular_function	protein binding
O	0005524	molecular_function	ATP binding
O	0005829	cellular_component	cytosol
O	0005975	biological_process	carbohydrate metabolic process
O	0006071	biological_process	glycerol metabolic process
O	0006072	biological_process	glycerol-3-phosphate metabolic process
O	0006974	biological_process	DNA damage response
O	0008270	molecular_function	zinc ion binding
O	0016301	molecular_function	kinase activity
O	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
O	0019563	biological_process	glycerol catabolic process
O	0042802	molecular_function	identical protein binding
O	0046872	molecular_function	metal ion binding
X	0004370	molecular_function	glycerol kinase activity
X	0005515	molecular_function	protein binding
X	0005524	molecular_function	ATP binding
X	0005829	cellular_component	cytosol
X	0005975	biological_process	carbohydrate metabolic process
X	0006071	biological_process	glycerol metabolic process
X	0006072	biological_process	glycerol-3-phosphate metabolic process
X	0006974	biological_process	DNA damage response
X	0008270	molecular_function	zinc ion binding
X	0016301	molecular_function	kinase activity
X	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
X	0019563	biological_process	glycerol catabolic process
X	0042802	molecular_function	identical protein binding
X	0046872	molecular_function	metal ion binding
Y	0004370	molecular_function	glycerol kinase activity
Y	0005515	molecular_function	protein binding
Y	0005524	molecular_function	ATP binding
Y	0005829	cellular_component	cytosol
Y	0005975	biological_process	carbohydrate metabolic process
Y	0006071	biological_process	glycerol metabolic process
Y	0006072	biological_process	glycerol-3-phosphate metabolic process
Y	0006974	biological_process	DNA damage response
Y	0008270	molecular_function	zinc ion binding
Y	0016301	molecular_function	kinase activity
Y	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
Y	0019563	biological_process	glycerol catabolic process
Y	0042802	molecular_function	identical protein binding
Y	0046872	molecular_function	metal ion binding
Z	0004370	molecular_function	glycerol kinase activity
Z	0005515	molecular_function	protein binding
Z	0005524	molecular_function	ATP binding
Z	0005829	cellular_component	cytosol
Z	0005975	biological_process	carbohydrate metabolic process
Z	0006071	biological_process	glycerol metabolic process
Z	0006072	biological_process	glycerol-3-phosphate metabolic process
Z	0006974	biological_process	DNA damage response
Z	0008270	molecular_function	zinc ion binding
Z	0016301	molecular_function	kinase activity
Z	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
Z	0019563	biological_process	glycerol catabolic process
Z	0042802	molecular_function	identical protein binding
Z	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 O 601

Chain	Residue
X	ASN228
X	GLY233
X	GLY234
X	ARG236
Z	ASP198
Z	ARG211
O	GLY233
O	GLY234
O	ARG236
O	HOH624
O	HOH652

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 Y 602

Chain	Residue
O	ASP198
O	ARG211
Y	GLY233
Y	GLY234
Y	ARG236
Y	HOH658
Z	GLY233
Z	GLY234
Z	ARG236
Z	HOH613

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADP O 607

Chain	Residue
O	THR13
O	ARG17
O	GLY266
O	THR267
O	GLY310
O	ALA311
O	ILE313
O	GLN314
O	ALA326
O	GLY411
O	ALA412
O	ASN415
O	HOH613
O	HOH630
O	HOH646

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ADP Y 608

Chain	Residue
Y	GLY12
Y	ARG17
Y	GLY266
Y	THR267
Y	GLY310
Y	ALA311
Y	ALA326
Y	GLY411
Y	ALA412
Y	ASN415
Y	HOH642
Y	HOH647
Y	HOH654

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ADP Z 609

Chain	Residue
Z	THR13
Z	ARG17
Z	GLY266
Z	THR267
Z	GLY310
Z	ALA311
Z	ALA326
Z	TYR327
Z	SER329
Z	GLY411
Z	ALA412
Z	ASN415
Z	HOH611
Z	HOH616
Z	HOH621
Z	HOH632
Z	HOH639
Z	HOH659

site_id	AC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP X 610

Chain	Residue
X	GLY12
X	THR13
X	ARG17
X	GLY266
X	THR267
X	GLY310
X	ALA311
X	ALA326
X	TYR327
X	GLY411
X	ALA412
X	HOH613
X	HOH616
X	HOH617
X	HOH639
X	HOH646

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL O 603

Chain	Residue
O	ARG83
O	GLU84
O	TYR135
O	ASP245
O	GLN246
O	PHE270

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL Y 604

Chain	Residue
Y	ASP245
Y	GLN246
Y	HOH642
Y	THR13
Y	GLN82
Y	ARG83
Y	GLU84
Y	TRP103
Y	TYR135

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL Z 605

Chain	Residue
Z	ASN81
Z	GLN82
Z	ARG83
Z	GLU84
Z	TYR135
Z	ASP245
Z	GLN246
Z	PHE270

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL X 606

Chain	Residue
X	GLN82
X	ARG83
X	GLU84
X	TRP103
X	TYR135
X	ASP245
X	GLN246
X	PHE270
X	HOH639

site_id	PO4
Number of Residues	4
Details

Chain	Residue
O	ARG236
Y	ARG236
Z	ARG236
X	ARG236

Functional Information from PROSITE/UniProt

site_id	PS00445
Number of Residues	21
Details	FGGY_KINASES_2 FGGY family of carbohydrate kinases signature 2. GaIFGLtrgvnan.HIIRATLE

Chain	Residue	Details
O	GLY362-GLU382

site_id	PS00933
Number of Residues	13
Details	FGGY_KINASES_1 FGGY family of carbohydrate kinases signature 1. YfSgtKVKWILDH

Chain	Residue	Details
O	TYR135-HIS147

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:8170944, ECO:0007744\|PDB:1GLC, ECO:0007744\|PDB:1GLD, ECO:0007744\|PDB:1GLE

Chain	Residue	Details
O	THR13
Y	TYR135
Y	ASP245
Y	GLU478
Z	THR13
Z	ARG83
Z	GLU84
Z	TYR135
Z	ASP245
Z	GLU478
X	THR13
O	ARG83
X	ARG83
X	GLU84
X	TYR135
X	ASP245
X	GLU478
O	GLU84
O	TYR135
O	ASP245
O	GLU478
Y	THR13
Y	ARG83
Y	GLU84

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305\|PubMed:10090737, ECO:0007744\|PDB:1BWF, ECO:0007744\|PDB:1GLJ, ECO:0007744\|PDB:1GLL

Chain	Residue	Details
O	THR14
O	GLY411
Y	THR14
Y	GLY411
Z	THR14
Z	GLY411
X	THR14
X	GLY411

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305\|PubMed:10090737, ECO:0007744\|PDB:1GLJ

Chain	Residue	Details
O	SER15
Y	SER15
Z	SER15
X	SER15

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:8170944, ECO:0000269\|PubMed:8430315, ECO:0000269\|PubMed:9817843, ECO:0007744\|PDB:1GLB, ECO:0007744\|PDB:1GLD, ECO:0007744\|PDB:1GLE, ECO:0007744\|PDB:1GLF

Chain	Residue	Details
O	ARG17
Y	ARG17
Z	ARG17
X	ARG17

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:9843423, ECO:0007744\|PDB:1BO5

Chain	Residue	Details
O	GLY234
O	ARG236
Y	GLY234
Y	ARG236
Z	GLY234
Z	ARG236
X	GLY234
X	ARG236

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:8430315, ECO:0000269\|PubMed:9843423, ECO:0007744\|PDB:1BO5, ECO:0007744\|PDB:1BOT

Chain	Residue	Details
O	GLN246
Y	GLN246
Z	GLN246
X	GLN246

site_id	SWS_FT_FI7
Number of Residues	12
Details	BINDING: BINDING => ECO:0000305\|PubMed:10090737, ECO:0007744\|PDB:1BWF, ECO:0007744\|PDB:1GLL

Chain	Residue	Details
O	THR267
X	THR267
X	GLY310
X	GLN314
O	GLY310
O	GLN314
Y	THR267
Y	GLY310
Y	GLN314
Z	THR267
Z	GLY310
Z	GLN314

site_id	SWS_FT_FI8
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:8170944, ECO:0000269\|PubMed:8430315, ECO:0007744\|PDB:1GLB, ECO:0007744\|PDB:1GLC, ECO:0007744\|PDB:1GLD, ECO:0007744\|PDB:1GLE

Chain	Residue	Details
O	ASN415
Y	ASN415
Z	ASN415
X	ASN415

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: N6-malonyllysine => ECO:0000269\|PubMed:21908771

Chain	Residue	Details
O	LYS232
Y	LYS232
Z	LYS232
X	LYS232

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