Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3UMP

Crystal structure of the Phosphofructokinase-2 from Escherichia coli in complex with Cesium and ATP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0003872	molecular_function	6-phosphofructokinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0006096	biological_process	glycolytic process
A	0006974	biological_process	DNA damage response
A	0008443	molecular_function	phosphofructokinase activity
A	0009024	molecular_function	tagatose-6-phosphate kinase activity
A	0016052	biological_process	carbohydrate catabolic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0044281	biological_process	small molecule metabolic process
A	0046835	biological_process	carbohydrate phosphorylation
A	0046872	molecular_function	metal ion binding
A	0061615	biological_process	glycolytic process through fructose-6-phosphate
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003872	molecular_function	6-phosphofructokinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0006096	biological_process	glycolytic process
B	0006974	biological_process	DNA damage response
B	0008443	molecular_function	phosphofructokinase activity
B	0009024	molecular_function	tagatose-6-phosphate kinase activity
B	0016052	biological_process	carbohydrate catabolic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0044281	biological_process	small molecule metabolic process
B	0046835	biological_process	carbohydrate phosphorylation
B	0046872	molecular_function	metal ion binding
B	0061615	biological_process	glycolytic process through fructose-6-phosphate

Functional Information from PDB Data

site_id	AC1
Number of Residues	30
Details	BINDING SITE FOR RESIDUE ATP A 313

Chain	Residue
A	LYS185
A	MET258
A	VAL280
A	GLY283
A	SER284
A	THR287
A	MG310
A	MG311
A	HOH320
A	HOH323
A	HOH326
A	ASN187
A	HOH354
A	HOH510
A	HOH512
A	HOH530
A	HOH532
A	HOH534
A	HOH535
A	HOH536
B	LYS27
B	ATP312
A	SER224
B	HOH358
A	LEU225
A	GLY226
A	PRO227
A	GLY229
A	ALA254
A	GLY255

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 310

Chain	Residue
A	ATP313
A	HOH534
A	HOH535
A	HOH536
B	HOH533

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 311

Chain	Residue
A	ATP313
A	HOH530
A	HOH532
B	ATP312

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CS A 315

Chain	Residue
A	SER250
A	VAL252
A	ALA286
A	ASN289
A	GLY291
A	ARG293

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 312

Chain	Residue
A	ATP314
A	HOH545
B	ATP313
B	HOH527

site_id	AC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP A 314

Chain	Residue
A	TYR23
A	PRO24
A	GLY26
A	LYS27
A	GLU102
A	MG312
A	HOH376
A	HOH411
A	HOH430
A	HOH494
A	HOH508
A	HOH529
A	HOH543
A	HOH544
A	HOH545
B	ASN187
B	LYS189
B	GLY226
B	THR251
B	ATP313

site_id	AC7
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP B 312

Chain	Residue
A	ASN187
A	GLY226
A	PRO227
A	MG311
A	ATP313
A	HOH463
A	HOH530
A	HOH532
B	TYR23
B	GLY26
B	LYS27
B	GLU102
B	HOH358
B	HOH386
B	HOH412
B	HOH418
B	HOH423
B	HOH494
B	HOH533
B	HOH534

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 311

Chain	Residue
A	HOH543
B	ATP313
B	HOH317
B	HOH448
B	HOH542

site_id	AC9
Number of Residues	29
Details	BINDING SITE FOR RESIDUE ATP B 313

Chain	Residue
B	LYS185
B	ASN187
B	SER224
B	LEU225
B	GLY226
B	PRO227
B	GLY229
B	ALA254
B	GLY255
B	MET258
B	VAL280
B	GLY283
B	SER284
B	THR287
B	MG311
B	HOH317
B	HOH321
B	HOH340
B	HOH349
B	HOH408
B	HOH433
B	HOH448
B	HOH527
B	HOH542
A	LYS27
A	MG312
A	ATP314
A	HOH411
A	HOH545

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CS B 315

Chain	Residue
B	SER250
B	VAL252
B	ALA286
B	ASN289
B	GLY291
B	ARG293

Functional Information from PROSITE/UniProt

site_id	PS00583
Number of Residues	25
Details	PFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. GGgGiNVAraIaHLGgsataifpaG

Chain	Residue	Details
A	GLY38-GLY62

site_id	PS00584
Number of Residues	14
Details	PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. STvGAGDsmvGAMT

Chain	Residue	Details
A	SER250-THR263

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18762190","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CQD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	20
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"18762190","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23823238","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Structure of E. coli PFK2 in complex with substrates and products.","authors":["Pereira H.M.","Caniuguir A.","Baez M.","Cabrera R.","Garratt R.C.","Babul J."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Structure of E. coli PFK2 mutant Y23D.","authors":["Pereira H.M.","Caniuguir A.","Baez M.","Cabrera R.","Garratt R.C.","Babul J."]}},{"source":"PDB","id":"3CQD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"18762190","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CQD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details