Structure of PDB 5oey Chain C

Receptor sequence

>5oeyC (length=326) Species: 5664 (Leishmania major)

PTPTTLTQYIIKSQPRGDFTLLMMAIQTSVKVIEKNIRRAGMKGMLGYIA
GANATGDHQAKLDVISNIAFKAYLLSSTSVCVLGSEEEEQMIIAESGRRG
DYLIFFDPLDGSSNIDANVSVGSIWGVWRLPKDTTINSVEDANAVIRMLK
GTDMVSAGYAVYGSATNLVLTSGHGVDGFTLDPNIGEFILTHPHISIPKK
RSIYSVNEGNYGKWEPWFKEYIDYLKMNKTTRYSARYIGSMVGDIHRTLL
YGGIFCYPKDANQVEGKLRLLYEAAPMAMIVEQAGGKAVGSNGRILEQSI
TRLHQRTPVYFGSRQEVDLCMAFRDR

3D structure

• PDB: 5oey Structures of Leishmania Fructose-1,6-Bisphosphatase Reveal Species-Specific Differences in the Mechanism of Allosteric Inhibition.
• Chain: C
• Resolution: 2.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D74 E97 E98 D118 L120 D121 E284
• Catalytic site (residue number reindexed from 1): D63 E86 E87 D107 L109 D110 E273
• 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	PO4	C	E97 D118 D121 G122 S123	E86 D107 D110 G111 S112
BS02	MN	C	E97 D118 L120 D121	E86 D107 L109 D110
BS03	MN	C	D118 D121 E284	D107 D110 E273

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

External links

• PDB: RCSB:5oey, PDBe:5oey, PDBj:5oey
• PDBsum: 5oey
• PubMed: 28882541
• UniProt: O97193