Structure of PDB 1dgk Chain N
Receptor sequence
>1dgkN (length=898) Species:
9606
(Homo sapiens) [
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DDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLP
TFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTP
ENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDE
AILITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMM
TCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFG
DDGSLEDIRTEFDRAIDAYSLNPGKQLFEKMVSGMYLGELVRLILVKMAK
EGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLGVEPSD
DDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGS
LYKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAE
QHRQIEETLAHFHLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSF
VRRTPDGTENGDFLALDLGGANFRVLLVKIRSGKKRTVEMHNKIYAIPIE
IMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGI
LITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVGTMMTC
AYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDN
GCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKG
FLFRGQISETLKTRGIFETKFLSQIESDRLALLQVRAILQQLGLNSTCDD
SILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLY
KLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKGAALITAVGVRLRT
3D structure
PDB
1dgk
Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation.
Chain
N
Resolution
2.8 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 D657
Catalytic site (residue number reindexed from 1)
R524 S588 D642
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
GLC
N
S155 F156 T172 K173 N208 D209 N235 E260 E294
S140 F141 T157 K158 N193 D194 N220 E245 E279
BS02
GLC
N
S603 F604 T620 K621 N656 D657 N683 E708 E742
S588 F589 T605 K606 N641 D642 N668 E693 E727
BS03
PO4
N
G87 S88 G231 T232 S415
G72 S73 G216 T217 S400
BS04
ADP
N
A536 N537 G679 T680 G747 T784 K785 S788 T863 L864 L867
A521 N522 G664 T665 G732 T769 K770 S773 T848 L849 L852
BS05
ADP
N
R30 H373 T376 F380 R425 R426
R15 H358 T361 F365 R410 R411
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
GO:0019158
mannokinase activity
GO:0042834
peptidoglycan binding
GO:0047931
glucosamine kinase activity
Biological Process
GO:0001678
intracellular glucose homeostasis
GO:0002720
positive regulation of cytokine production involved in immune response
GO:0005975
carbohydrate metabolic process
GO:0006002
fructose 6-phosphate metabolic process
GO:0006006
glucose metabolic process
GO:0006013
mannose metabolic process
GO:0006096
glycolytic process
GO:0006954
inflammatory response
GO:0009298
GDP-mannose biosynthetic process
GO:0016310
phosphorylation
GO:0019318
hexose metabolic process
GO:0032731
positive regulation of interleukin-1 beta production
GO:0045087
innate immune response
GO:0046835
carbohydrate phosphorylation
GO:0051156
glucose 6-phosphate metabolic process
GO:0061621
canonical glycolysis
GO:0061728
GDP-mannose biosynthetic process from mannose
GO:0072655
establishment of protein localization to mitochondrion
GO:0072656
maintenance of protein location in mitochondrion
GO:0141199
GDP-mannose biosynthetic process from glucose
GO:1901135
carbohydrate derivative metabolic process
Cellular Component
GO:0005737
cytoplasm
GO:0005739
mitochondrion
GO:0005741
mitochondrial outer membrane
GO:0005829
cytosol
GO:0045121
membrane raft
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:1dgk
,
PDBe:1dgk
,
PDBj:1dgk
PDBsum
1dgk
PubMed
10686099
UniProt
P19367
|HXK1_HUMAN Hexokinase-1 (Gene Name=HK1)
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