Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4F9O

Crystal Structure of recombinant human Hexokinase type I with 2-deoxy-Glucose 6-Phosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001678	biological_process	intracellular glucose homeostasis
A	0002720	biological_process	positive regulation of cytokine production involved in immune response
A	0004340	molecular_function	glucokinase activity
A	0004396	molecular_function	hexokinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005536	molecular_function	D-glucose binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005741	cellular_component	mitochondrial outer membrane
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006006	biological_process	glucose metabolic process
A	0006013	biological_process	mannose metabolic process
A	0006096	biological_process	glycolytic process
A	0006954	biological_process	inflammatory response
A	0008865	molecular_function	fructokinase activity
A	0016301	molecular_function	kinase activity
A	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
A	0019158	molecular_function	mannokinase activity
A	0019318	biological_process	hexose metabolic process
A	0032731	biological_process	positive regulation of interleukin-1 beta production
A	0042834	molecular_function	peptidoglycan binding
A	0045087	biological_process	innate immune response
A	0045121	cellular_component	membrane raft
A	0046835	biological_process	carbohydrate phosphorylation
A	0047931	molecular_function	glucosamine kinase activity
A	0051156	biological_process	glucose 6-phosphate metabolic process
A	0061621	biological_process	canonical glycolysis
A	0072655	biological_process	establishment of protein localization to mitochondrion
A	0072656	biological_process	maintenance of protein location in mitochondrion
A	1901135	biological_process	carbohydrate derivative metabolic process
B	0001678	biological_process	intracellular glucose homeostasis
B	0002720	biological_process	positive regulation of cytokine production involved in immune response
B	0004340	molecular_function	glucokinase activity
B	0004396	molecular_function	hexokinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005536	molecular_function	D-glucose binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005741	cellular_component	mitochondrial outer membrane
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0006002	biological_process	fructose 6-phosphate metabolic process
B	0006006	biological_process	glucose metabolic process
B	0006013	biological_process	mannose metabolic process
B	0006096	biological_process	glycolytic process
B	0006954	biological_process	inflammatory response
B	0008865	molecular_function	fructokinase activity
B	0016301	molecular_function	kinase activity
B	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
B	0019158	molecular_function	mannokinase activity
B	0019318	biological_process	hexose metabolic process
B	0032731	biological_process	positive regulation of interleukin-1 beta production
B	0042834	molecular_function	peptidoglycan binding
B	0045087	biological_process	innate immune response
B	0045121	cellular_component	membrane raft
B	0046835	biological_process	carbohydrate phosphorylation
B	0047931	molecular_function	glucosamine kinase activity
B	0051156	biological_process	glucose 6-phosphate metabolic process
B	0061621	biological_process	canonical glycolysis
B	0072655	biological_process	establishment of protein localization to mitochondrion
B	0072656	biological_process	maintenance of protein location in mitochondrion
B	1901135	biological_process	carbohydrate derivative metabolic process

Functional Information from PROSITE/UniProt

site_id	PS00378
Number of Residues	26
Details	HEXOKINASE_1 Hexokinase domain signature. VGFTFSFPcqqskIDeaiLitWTKrF

Chain	Residue	Details
A	VAL150-PHE175
A	LEU598-PHE623

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:10574795, ECO:0000269\|PubMed:10686099, ECO:0007744\|PDB:1CZA, ECO:0007744\|PDB:1DGK, ECO:0007744\|PDB:1QHA

Chain	Residue	Details
A	ARG30
A	ARG425
B	ARG30
B	ARG425

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:10686099, ECO:0000269\|PubMed:9735292, ECO:0007744\|PDB:1DGK, ECO:0007744\|PDB:1HKC

Chain	Residue	Details
A	ASP84
A	THR863
B	ASP84
B	THR863

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10686099, ECO:0000269\|PubMed:9493266, ECO:0000269\|PubMed:9735292, ECO:0007744\|PDB:1DGK, ECO:0007744\|PDB:1HKB, ECO:0007744\|PDB:1HKC, ECO:0007744\|PDB:4F9O, ECO:0007744\|PDB:4FOE, ECO:0007744\|PDB:4FOI, ECO:0007744\|PDB:4FPA

Chain	Residue	Details
A	SER155
B	SER155

site_id	SWS_FT_FI4
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269\|PubMed:10574795, ECO:0000269\|PubMed:10686099, ECO:0000269\|PubMed:9493266, ECO:0000269\|PubMed:9735292, ECO:0007744\|PDB:1CZA, ECO:0007744\|PDB:1DGK, ECO:0007744\|PDB:1HKB, ECO:0007744\|PDB:1HKC, ECO:0007744\|PDB:1QHA, ECO:0007744\|PDB:4F9O, ECO:0007744\|PDB:4FOE, ECO:0007744\|PDB:4FOI, ECO:0007744\|PDB:4FPA, ECO:0007744\|PDB:4FPB

Chain	Residue	Details
A	THR172
B	GLN291
A	ASN208
A	ASN235
A	GLU260
A	GLN291
B	THR172
B	ASN208
B	ASN235
B	GLU260

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10574795, ECO:0000269\|PubMed:10686099, ECO:0000269\|PubMed:9493266, ECO:0007744\|PDB:1CZA, ECO:0007744\|PDB:1HKB, ECO:0007744\|PDB:1QHA, ECO:0007744\|PDB:4FOE, ECO:0007744\|PDB:4FOI, ECO:0007744\|PDB:4FPA

Chain	Residue	Details
A	ASP209
B	ASP209

site_id	SWS_FT_FI6
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269\|PubMed:10574795, ECO:0000269\|PubMed:10686099, ECO:0000269\|PubMed:9493266, ECO:0007744\|PDB:1CZA, ECO:0007744\|PDB:1HKB, ECO:0007744\|PDB:1QHA, ECO:0007744\|PDB:4F9O, ECO:0007744\|PDB:4FOE, ECO:0007744\|PDB:4FOI, ECO:0007744\|PDB:4FPA, ECO:0007744\|PDB:4FPB

Chain	Residue	Details
A	THR232
B	ASP861
A	ASP413
A	SER449
A	THR680
A	ASP861
B	THR232
B	ASP413
B	SER449
B	THR680

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10574795, ECO:0007744\|PDB:1QHA

Chain	Residue	Details
A	ASN345
B	ASN345

site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10574795, ECO:0000269\|PubMed:10686099, ECO:0007744\|PDB:1CZA, ECO:0007744\|PDB:1QHA, ECO:0007744\|PDB:4FOE, ECO:0007744\|PDB:4FOI, ECO:0007744\|PDB:4FPA

Chain	Residue	Details
A	ASP532
B	ASP532

site_id	SWS_FT_FI9
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10686099, ECO:0000269\|PubMed:9493266, ECO:0007744\|PDB:1DGK, ECO:0007744\|PDB:1HKB, ECO:0007744\|PDB:4F9O, ECO:0007744\|PDB:4FOE, ECO:0007744\|PDB:4FOI, ECO:0007744\|PDB:4FPA, ECO:0007744\|PDB:4FPB

Chain	Residue	Details
A	SER603
B	SER603

site_id	SWS_FT_FI10
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269\|PubMed:10574795, ECO:0000269\|PubMed:10686099, ECO:0000269\|PubMed:9493266, ECO:0007744\|PDB:1CZA, ECO:0007744\|PDB:1DGK, ECO:0007744\|PDB:1HKB, ECO:0007744\|PDB:1QHA, ECO:0007744\|PDB:4F9O, ECO:0007744\|PDB:4FOE, ECO:0007744\|PDB:4FOI, ECO:0007744\|PDB:4FPA, ECO:0007744\|PDB:4FPB

Chain	Residue	Details
A	THR620
B	GLU742
A	ASN656
A	SER682
A	GLU708
A	GLU742
B	THR620
B	ASN656
B	SER682
B	GLU708

site_id	SWS_FT_FI11
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10574795, ECO:0000269\|PubMed:10686099, ECO:0000269\|PubMed:9493266, ECO:0007744\|PDB:1CZA, ECO:0007744\|PDB:1HKB, ECO:0007744\|PDB:1QHA, ECO:0007744\|PDB:4FOI, ECO:0007744\|PDB:4FPA

Chain	Residue	Details
A	ASP657
B	ASP657

site_id	SWS_FT_FI12
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:10686099, ECO:0007744\|PDB:1DGK

Chain	Residue	Details
A	GLY747
A	THR784
B	GLY747
B	THR784

site_id	SWS_FT_FI13
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10574795, ECO:0000269\|PubMed:10686099, ECO:0000269\|PubMed:9493266, ECO:0007744\|PDB:1CZA, ECO:0007744\|PDB:1HKB, ECO:0007744\|PDB:1QHA, ECO:0007744\|PDB:4F9O, ECO:0007744\|PDB:4FOI, ECO:0007744\|PDB:4FPA, ECO:0007744\|PDB:4FPB

Chain	Residue	Details
A	SER897
B	SER897

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: N-acetylmethionine => ECO:0000269\|Ref.7, ECO:0007744\|PubMed:19413330, ECO:0007744\|PubMed:25944712

Chain	Residue	Details
A	MET1
B	MET1

site_id	SWS_FT_FI15
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P05708

Chain	Residue	Details
A	SER337
B	SER337

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 696

Chain	Residue	Details
A	ARG539	electrostatic stabiliser, polar interaction
A	SER603	electrostatic stabiliser, polar interaction
A	ASP657	proton acceptor, proton donor

site_id	MCSA2
Number of Residues	3
Details	M-CSA 696

Chain	Residue	Details
B	ARG539	electrostatic stabiliser, polar interaction
B	SER603	electrostatic stabiliser, polar interaction
B	ASP657	proton acceptor, proton donor

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