Structure of PDB 3pr3 Chain A

Receptor sequence
>3pr3A (length=578) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
NMEITNLKSYKELVTLSAEEKTKDLKDYLNDKNRSESLIKKFKNFYMDLS
RQRYSEKTLNKLVEYAEEVELKKKVEKTFMGEKVNMTENRSVLHTALRIP
IEKINTHKIIIDNKNVLEDVHGVLKKIEKYSDDIRNGVIKTCKNTKFKNV
ICIGIGGSYLGTEFVYEAMKYYYYNMELNKNEKDQVNNFNNNYDQDNVFN
VRFLANVDPNDVNRAIQNLDQYDTLVIIISKTFTTAETMLNARSIKKWLS
LKIKDDENLSKHMVAVSTNLKLTDEFGISRDNVFEFWDWVGGRFSVTSSV
GILPLSIAFGYKNMRNFLNGCHDMDEHFLHADLKENIPVLLALTSFYNSH
FFDYKNVAILPYFQNLLKFSAHIQQLSMESNGKSVDRNNQPIHYNTCQVY
FGEPGTNGQHSFYQLIHQGQVIPVELIGFKHSHFPIKFDKEVVSNHDELM
TNFFAQADALAIGKTYEQVKEENEKNKMSPELLTHKVFNGNRPSTLLLFD
ELNFYTCGLLLSLYESRIVAEGFLLNINSFDQWGVELGKVLAKEVRNYFN
DTRNQKKSDNTYNFNESTKILLNYYLSK
3D structure
PDB3pr3 Crystal structure of Plasmodium falciparum glucose-6-phosphate isomerase (PF14_0341) in complex with fructose-6-phosphate
ChainA
Resolution2.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K232 E238 G293 R294 E380 H411 K540
Catalytic site (residue number reindexed from 1) K231 E237 G292 R293 E379 H410 K539
Enzyme Commision number 5.3.1.9: glucose-6-phosphate isomerase.
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 F6P A G158 S231 K232 T233 T236 Q376 E380 G157 S230 K231 T232 T235 Q375 E379
Gene Ontology
Molecular Function
GO:0004347 glucose-6-phosphate isomerase activity
GO:0016853 isomerase activity
GO:0048029 monosaccharide binding
GO:0097367 carbohydrate derivative binding
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0006098 pentose-phosphate shunt
GO:0051156 glucose 6-phosphate metabolic process
GO:1901135 carbohydrate derivative metabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3pr3, PDBe:3pr3, PDBj:3pr3
PDBsum3pr3
PubMed
UniProtQ8ILA4

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