Structure of PDB 5ofu Chain A

Receptor sequence
>5ofuA (length=322) Species: 5664 (Leishmania major) [Search protein sequence]
PTPTTLTQYIIKSQPPHSRGDFTLLMMAIQTSVKVIEKNIRRAGMKGMLG
YIAGAKLDVISNIAFKAYLLSSTSVCVLGSEEEEQMIIAESGRRGDYLIF
FDPLDGSSNIDANVSVGSIWGVWRLPKDTTINSVEDANAVIRMLKGTDMV
SAGYAVYGSATNLVLTSGHGVDGFTLDPNIGEFILTHPHISIPKKRSIYS
VNEGNYGKWEPWFKEYIDYLKMNKTTRYSARYIGSMVGDIHRTLLYGGIF
CYPKDANQVEGKLRLLYEAAPMAMIVEQAGGKAVGSNGRILEQSITRLHQ
RTPVYFGSRQEVDLCMAFRDRN
3D structure
PDB5ofu Structures of Leishmania Fructose-1,6-Bisphosphatase Reveal Species-Specific Differences in the Mechanism of Allosteric Inhibition.
ChainA
Resolution2.62 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D74 E97 E98 D118 L120 D121 E284
Catalytic site (residue number reindexed from 1) D58 E81 E82 D102 L104 D105 E268
Enzyme Commision number 3.1.3.11: fructose-bisphosphatase.
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 AMP A I16 S19 Q20 P21 S24 R25 G26 F28 Y113 I10 S13 Q14 P15 S18 R19 G20 F22 Y97 PDBbind-CN: -logKd/Ki=4.20,Ki=63.8uM
BS02 F6P A D121 G122 Y248 S251 M252 Y268 K278 D105 G106 Y232 S235 M236 Y252 K262
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0042132 fructose 1,6-bisphosphate 1-phosphatase activity
GO:0042578 phosphoric ester hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005986 sucrose biosynthetic process
GO:0006000 fructose metabolic process
GO:0006002 fructose 6-phosphate metabolic process
GO:0006094 gluconeogenesis
GO:0030388 fructose 1,6-bisphosphate metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0020015 glycosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5ofu, PDBe:5ofu, PDBj:5ofu
PDBsum5ofu
PubMed28882541
UniProtO97193

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