Structure of PDB 2bh9 Chain A

Receptor sequence
>2bh9A (length=489) Species: 9606 (Homo sapiens) [Search protein sequence]
VQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPENTFIVGYARSRLT
VADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQRLNSHMN
ALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRD
LQSSDRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWN
RDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKP
ASTNSDDVRDEKVKVLKCISEVQANNVVLGQYVGNPDGEGEATKGYLDDP
TVPRGSTTATFAAVVLYVENERWDGVPFILRCGKALNERKAEVRLQFHDV
AGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGN
RYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEK
PKPIPYIYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL
3D structure
PDB2bh9 Structural Studies of Glucose-6-Phosphate and Nadp+ Binding to Human Glucose-6-Phosphate Dehydrogenase
ChainA
Resolution2.5 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) D174 H175 H237
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 G38 S40 G41 L43 R72 S73 Y112 A141 L142 P143 E170 K171 G12 S14 G15 L17 R46 S47 Y86 A115 L116 P117 E144 K145
BS02 NAP A K366 R370 R393 Y401 K403 D421 R487 D493 F501 Y503 Y507 W509 K340 R344 R367 Y375 K377 D395 R461 D467 F475 Y477 Y481 W483
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:2bh9, PDBe:2bh9, PDBj:2bh9
PDBsum2bh9
PubMed15858258
UniProtP11413|G6PD_HUMAN Glucose-6-phosphate 1-dehydrogenase (Gene Name=G6PD)

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