Structure of PDB 1qki Chain A

Receptor sequence
>1qkiA (length=488) Species: 9606 (Homo sapiens) [Search protein sequence]
VCGHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPENTFIVGYARS
RLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQRLNS
HMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPF
GRDLQSSDRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGP
IWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAM
EKPASTNSDDVRDEKVKVLKCISEVQANNVVLGQYVGNPDGEGEATKGYL
DDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGKALNERKAEVRLQF
HDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLT
YGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELLEAWRIFTPLLHQIE
LEKPKPIPYIYGSRGPTEADELMKRVGFQYEGTYKWVN
3D structure
PDB1qki Human Glucose-6-Phosphate Dehydrogenase: The Crystal Structure Reveals a Structural Nadp+ Molecule and Provides Insights Into Enzyme Deficiency
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D200 H201 H263
Catalytic site (residue number reindexed from 1) D177 H178 H240
Enzyme Commision number 1.1.1.49: glucose-6-phosphate dehydrogenase (NADP(+)).
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 NAP A K238 R357 K366 R370 R393 Y401 R487 D493 M496 Y503 W509 K215 R334 K343 R347 R370 Y378 R464 D470 M473 Y480 W486
Gene Ontology
Molecular Function
GO:0004345 glucose-6-phosphate dehydrogenase activity
GO:0005515 protein binding
GO:0005536 D-glucose binding
GO:0016491 oxidoreductase activity
GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
GO:0030246 carbohydrate binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0050661 NADP binding
Biological Process
GO:0006006 glucose metabolic process
GO:0006098 pentose-phosphate shunt
GO:0006629 lipid metabolic process
GO:0006695 cholesterol biosynthetic process
GO:0006739 NADP metabolic process
GO:0006740 NADPH regeneration
GO:0006749 glutathione metabolic process
GO:0009051 pentose-phosphate shunt, oxidative branch
GO:0010041 response to iron(III) ion
GO:0010734 negative regulation of protein glutathionylation
GO:0014070 response to organic cyclic compound
GO:0019322 pentose biosynthetic process
GO:0021762 substantia nigra development
GO:0032094 response to food
GO:0034599 cellular response to oxidative stress
GO:0043249 erythrocyte maturation
GO:0043523 regulation of neuron apoptotic process
GO:0045471 response to ethanol
GO:0046390 ribose phosphate biosynthetic process
GO:0051156 glucose 6-phosphate metabolic process
GO:0061052 negative regulation of cell growth involved in cardiac muscle cell development
GO:1904879 positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel
GO:2000378 negative regulation of reactive oxygen species metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0009898 cytoplasmic side of plasma membrane
GO:0016020 membrane
GO:0034451 centriolar satellite
GO:0043231 intracellular membrane-bounded organelle
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1qki, PDBe:1qki, PDBj:1qki
PDBsum1qki
PubMed10745013
UniProtP11413|G6PD_HUMAN Glucose-6-phosphate 1-dehydrogenase (Gene Name=G6PD)

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