Structure of PDB 5hfu Chain A

Receptor sequence
>5hfuA (length=895) Species: 9606 (Homo sapiens) [Search protein sequence]
DQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPT
FVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPE
DIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDES
FLVSWTKGFKSSGVEGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMT
CGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGD
DGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKE
ELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLGLDPTQE
DCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSV
YKKHPHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQ
HRARQKTLEHLQLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYV
CATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWGGVEMHNKIYAIPQEV
MHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESIL
LKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCG
FEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNG
CLDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGL
LFRGRISERLKTRGIFETKFLSQIESDCLALLQVRAILQHLGLESTCDDS
IIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYK
LHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI
3D structure
PDB5hfu Discovery of a Novel 2,6-Disubstituted Glucosamine Series of Potent and Selective Hexokinase 2 Inhibitors.
ChainA
Resolution2.923 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R539 S603 K618 D657
Catalytic site (residue number reindexed from 1) R523 S587 K602 D641
Enzyme Commision number 2.7.1.1: hexokinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 603 A K62 S155 P157 C158 N208 D209 G233 N235 E260 Q291 E294 K46 S139 P141 C142 N192 D193 G217 N219 E244 Q275 E278 PDBbind-CN: -logKd/Ki=6.89,IC50=0.13uM
BS02 603 A K621 N656 D657 I677 G681 S682 N683 E708 Q739 E742 K605 N640 D641 I661 G665 S666 N667 E692 Q723 E726 PDBbind-CN: -logKd/Ki=6.89,IC50=0.13uM
Gene Ontology
Molecular Function
GO:0004340 glucokinase activity
GO:0004396 hexokinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0005536 D-glucose binding
GO:0008865 fructokinase activity
GO:0016301 kinase activity
GO:0016773 phosphotransferase activity, alcohol group as acceptor
Biological Process
GO:0001666 response to hypoxia
GO:0001678 intracellular glucose homeostasis
GO:0002931 response to ischemia
GO:0005975 carbohydrate metabolic process
GO:0006002 fructose 6-phosphate metabolic process
GO:0006006 glucose metabolic process
GO:0006096 glycolytic process
GO:0007595 lactation
GO:0008637 apoptotic mitochondrial changes
GO:0016310 phosphorylation
GO:0019318 hexose metabolic process
GO:0035795 negative regulation of mitochondrial membrane permeability
GO:0045766 positive regulation of angiogenesis
GO:0046324 regulation of D-glucose import
GO:0046835 carbohydrate phosphorylation
GO:0051156 glucose 6-phosphate metabolic process
GO:0061621 canonical glycolysis
GO:0072655 establishment of protein localization to mitochondrion
GO:0072656 maintenance of protein location in mitochondrion
GO:1901135 carbohydrate derivative metabolic process
GO:1990830 cellular response to leukemia inhibitory factor
GO:2000378 negative regulation of reactive oxygen species metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005741 mitochondrial outer membrane
GO:0005813 centrosome
GO:0005829 cytosol
GO:0016020 membrane
GO:0016529 sarcoplasmic reticulum
GO:0043231 intracellular membrane-bounded organelle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5hfu, PDBe:5hfu, PDBj:5hfu
PDBsum5hfu
PubMed26985301
UniProtP52789|HXK2_HUMAN Hexokinase-2 (Gene Name=HK2)

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