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3BIH

Crystal structure of fructose-1,6-bisphosphatase from E.coli GlpX

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006071biological_processglycerol metabolic process
A0006094biological_processgluconeogenesis
A0016787molecular_functionhydrolase activity
A0030145molecular_functionmanganese ion binding
A0030388biological_processfructose 1,6-bisphosphate metabolic process
A0042132molecular_functionfructose 1,6-bisphosphate 1-phosphatase activity
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX A 400
ChainResidue
AASP85
AILE87
AHOH455
AHOH520

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:19073594
ChainResidueDetails
AASP33
AGLU57
AASP85
AGLU88
AGLU213

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19073594
ChainResidueDetails
ATYR119
ALYS164
AASP186
AGLY210

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PDB entries from 2024-07-17

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