Structure of PDB 3rpl Chain B

Receptor sequence

>3rplB (length=349) Species: 1148 (Synechocystis sp. PCC 6803)

GRGSVDSTLGLEIIEVVEQAAIASAKWMGKGEKNTADQVAVEAMRERMNK
IHMRGRIVIGEGERDDAPMLYIGEEVGICTREDAKSFCNPDELVEIDIAV
DPCEGTNLVAYGQNGSMAVLAISEKGGLFAAPDFYMKKLAAPPAAKGHVD
IDKSATENLKILSDCLNRSIEELVVVVMDRPRHKELIQEIRNAGARVRLI
SDGDVSAAISCAFSGTNIHALMGIGAAPEGVISAAAMRCLGGHFQGQLIY
DPEVVKTGLIGESREGNLERLASMGIKNPDQVYNCEELACGETVLFAACG
ITPGTLMEGVRFFHGGVRTQSLVISSQSSTARFVDTVHMKESPKVIQLH

3D structure

• PDB: 3rpl New insights into the structural and interactional basis for a promising route towards fructose-1,6-/sedoheptulose-1,7-bisphosphatases controlling
• Chain: B
• Resolution: 2.4 Å

Enzymatic activity

• Enzyme Commision number: 3.1.3.11: fructose-bisphosphatase.
  3.1.3.37: sedoheptulose-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	B	R164 G211 N213 H215	R168 G215 N217 H219
BS02	AMP	B	R307 F309 R314 V341 Q343 H345	R311 F313 R318 V345 Q347 H349
BS03	MG	B	D97 E100 E225	D101 E104 E229
BS04	MG	B	D33 E57 C99	D37 E61 C103
BS05	FBP	B	E100 G101 T102 Y131 M174 R176 R178 D198 G199 D200 A222	E104 G105 T106 Y135 M178 R180 R182 D202 G203 D204 A226

Gene Ontology

Molecular Function

• GO:0016787 hydrolase activity
• GO:0042132 fructose 1,6-bisphosphate 1-phosphatase activity
• GO:0046872 metal ion binding
• GO:0050278 sedoheptulose-bisphosphatase activity

Biological Process

• GO:0006071 glycerol metabolic process
• GO:0006094 gluconeogenesis
• GO:0019253 reductive pentose-phosphate cycle
• GO:0030388 fructose 1,6-bisphosphate metabolic process

External links

• PDB: RCSB:3rpl, PDBe:3rpl, PDBj:3rpl
• PDBsum: 3rpl
• UniProt: P73922|FBSB_SYNY3 D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase (Gene Name=slr2094)