Structure of PDB 3pr3 Chain B

Receptor sequence
>3pr3B (length=577) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
MEITNLKSYKELVTLSAEEKTKDLKDYLNDKNRSESLIKKFKNFYMDLSR
QRYSEKTLNKLVEYAEEVELKKKVEKTFMGEKVNMTENRSVLHTALRIPI
EKINTHKIIIDNKNVLEDVHGVLKKIEKYSDDIRNGVIKTCKNTKFKNVI
CIGIGGSYLGTEFVYEAMKYYYYNMELNKNEKDQVNNFNNNYDQDNVFNV
RFLANVDPNDVNRAIQNLDQYDTLVIIISKTFTTAETMLNARSIKKWLSL
KIKDDENLSKHMVAVSTNLKLTDEFGISRDNVFEFWDWVGGRFSVTSSVG
ILPLSIAFGYKNMRNFLNGCHDMDEHFLHADLKENIPVLLALTSFYNSHF
FDYKNVAILPYFQNLLKFSAHIQQLSMESNGKSVDRNNQPIHYNTCQVYF
GEPGTNGQHSFYQLIHQGQVIPVELIGFKHSHFPIKFDKEVVSNHDELMT
NFFAQADALAIGKTYEQVKEENEKNKMSPELLTHKVFNGNRPSTLLLFDE
LNFYTCGLLLSLYESRIVAEGFLLNINSFDQWGVELGKVLAKEVRNYFND
TRNQKKSDNTYNFNESTKILLNYYLSK
3D structure
PDB3pr3 Crystal structure of Plasmodium falciparum glucose-6-phosphate isomerase (PF14_0341) in complex with fructose-6-phosphate
ChainB
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) K230 E236 G291 R292 E378 H409 K538
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 B I156 G158 S231 K232 T233 T236 Q376 E380 I154 G156 S229 K230 T231 T234 Q374 E378
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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