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4HE0

Crystal structure of human muscle fructose-1,6-bisphosphatase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006000biological_processfructose metabolic process
A0006094biological_processgluconeogenesis
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0030018cellular_componentZ disc
A0042132molecular_functionfructose 1,6-bisphosphate 1-phosphatase activity
A0042578molecular_functionphosphoric ester hydrolase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0070161cellular_componentanchoring junction
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 A 401
ChainResidue
AASP68
AMG402
AMG403
AMG404
AGLU97
AASP118
ALEU120
AASP121
AGLY122
ASER123
AARG276
AGLU280

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AGLU97
AASP118
AASP121
AARG276
AGLU280
APO4401
AMG403

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
AGLU97
AASP118
ALEU120
APO4401
AMG402
AHOH547

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 404
ChainResidue
AASN64
AASP68
AGLU97
APO4401

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 405
ChainResidue
ASER131
ASER131

Functional Information from PROSITE/UniProt
site_idPS00124
Number of Residues13
DetailsFBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcnPVA
ChainResidueDetails
AGLY273-ALA285

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"source":"PubMed","id":"19626708","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22120740","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues15
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Important for the conversion from active R-state to inactive T-state in the presence of AMP"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9Z1N1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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