Structure of PDB 2fli Chain J

Receptor sequence

>2fliJ (length=218) Species: 1314 (Streptococcus pyogenes)

STLKIAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGAD
VVASMRKHSKLVFDCHLMVVDPERYVEAFAQAGADIMTIHTESTRHIHGA
LQKIKAAGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIP
ECLEKVATVAKWRDEKGLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYL
FKASDLVSQVQTLRTALN

3D structure

• PDB: 2fli d-Ribulose 5-Phosphate 3-Epimerase: Functional and Structural Relationships to Members of the Ribulose-Phosphate Binding (beta/alpha)(8)-Barrel Superfamily(,).
• Chain: J
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S9 H34 D36 M38 H67 M69 M138 D176
• Catalytic site (residue number reindexed from 1): S8 H33 D35 M37 H66 M68 M137 D175
• Enzyme Commision number: 5.1.3.1: ribulose-phosphate 3-epimerase.

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	ZN	J	H34 D36 H67 D176	H33 D35 H66 D175
BS02	DX5	J	S9 L11 D36 M69 P142 G145 D176 G177 G198 S199	S8 L10 D35 M68 P141 G144 D175 G176 G197 S198

Gene Ontology

Molecular Function

• GO:0004750 D-ribulose-phosphate 3-epimerase activity
• GO:0016853 isomerase activity
• GO:0016857 racemase and epimerase activity, acting on carbohydrates and derivatives
• GO:0046872 metal ion binding

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0006098 pentose-phosphate shunt
• GO:0009052 pentose-phosphate shunt, non-oxidative branch
• GO:0019323 pentose catabolic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:2fli, PDBe:2fli, PDBj:2fli
• PDBsum: 2fli
• PubMed: 16489742
• UniProt: Q9A1H8