Structure of PDB 3ifc Chain D

Receptor sequence
>3ifcD (length=319) Species: 9606 (Homo sapiens) [Search protein sequence]
DMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYG
IAGVKKLDVLSNSLVINMLQSSYSTCVLVSEENKDAIITAKEKRGKYVVC
FDPLDGSSNIDCLASIGTIFAIYRKTSDEPSEKDALQCGRNIVAAGYALY
GSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAK
YFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVHRTLVYGGIFLYPAN
QKSPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQRVPLI
LGSPEDVQEYLTCVQKNQA
3D structure
PDB3ifc Structure of E69Q mutant of human muscle fructose-1,6-bisphosphatase
ChainD
Resolution1.97 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 E280
Catalytic site (residue number reindexed from 1) D58 E81 E82 D102 L104 D105 E263
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 D V17 K20 G21 A24 G26 T27 G28 E29 L30 K112 Y113 R140 T177 V9 K12 G13 A16 G18 T19 G20 E21 L22 K96 Y97 R124 T160
BS02 P6P D D121 N212 Y215 Y244 G246 S247 M248 Y264 K274 D105 N195 Y198 Y227 G229 S230 M231 Y247 K257
Gene Ontology
Molecular Function
GO:0005515 protein 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:0042802 identical protein binding
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:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0030018 Z disc
GO:0070062 extracellular exosome
GO:0070161 anchoring junction

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ifc, PDBe:3ifc, PDBj:3ifc
PDBsum3ifc
PubMed22120740
UniProtO00757|F16P2_HUMAN Fructose-1,6-bisphosphatase isozyme 2 (Gene Name=FBP2)

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