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5OEY

Crystal structure of Leishmania major fructose-1,6-bisphosphatase in holo form.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006094biological_processgluconeogenesis
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0020015cellular_componentglycosome
A0042132molecular_functionfructose 1,6-bisphosphate 1-phosphatase activity
A0042578molecular_functionphosphoric ester hydrolase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006094biological_processgluconeogenesis
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0020015cellular_componentglycosome
B0042132molecular_functionfructose 1,6-bisphosphate 1-phosphatase activity
B0042578molecular_functionphosphoric ester hydrolase activity
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005975biological_processcarbohydrate metabolic process
C0006094biological_processgluconeogenesis
C0016787molecular_functionhydrolase activity
C0016791molecular_functionphosphatase activity
C0020015cellular_componentglycosome
C0042132molecular_functionfructose 1,6-bisphosphate 1-phosphatase activity
C0042578molecular_functionphosphoric ester hydrolase activity
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005975biological_processcarbohydrate metabolic process
D0006094biological_processgluconeogenesis
D0016787molecular_functionhydrolase activity
D0016791molecular_functionphosphatase activity
D0020015cellular_componentglycosome
D0042132molecular_functionfructose 1,6-bisphosphate 1-phosphatase activity
D0042578molecular_functionphosphoric ester hydrolase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue PO4 A 701
ChainResidue
AASP68
AMN702
AMN703
AK704
AGLU97
AASP118
ALEU120
AASP121
AGLY122
ASER123
AARG280
AGLU284

site_idAC2
Number of Residues7
Detailsbinding site for residue MN A 702
ChainResidue
AASP74
AGLU97
AGLU98
AASP118
ALEU120
APO4701
AK704

site_idAC3
Number of Residues4
Detailsbinding site for residue MN A 703
ChainResidue
AASP118
AASP121
AGLU284
APO4701

site_idAC4
Number of Residues4
Detailsbinding site for residue K A 704
ChainResidue
AASP68
AGLU97
APO4701
AMN702

site_idAC5
Number of Residues11
Detailsbinding site for residue PO4 B 701
ChainResidue
BGLU97
BASP118
BASP121
BGLY122
BSER123
BGLU284
BMN702
BMN703
BK704
DLYS210
DHOH801

site_idAC6
Number of Residues9
Detailsbinding site for residue MN B 702
ChainResidue
BGLU97
BGLU98
BASP118
BLEU120
BPO4701
BMN703
BHOH801
DLYS210
DHOH801

site_idAC7
Number of Residues6
Detailsbinding site for residue MN B 703
ChainResidue
BGLU97
BASP118
BASP121
BGLU284
BPO4701
BMN702

site_idAC8
Number of Residues2
Detailsbinding site for residue K B 704
ChainResidue
BPO4701
DGLN326

site_idAC9
Number of Residues12
Detailsbinding site for residue PO4 C 701
ChainResidue
CASP68
CGLU97
CASP118
CLEU120
CASP121
CGLY122
CSER123
CARG280
CGLU284
CMN702
CMN703
CK704

site_idAD1
Number of Residues7
Detailsbinding site for residue MN C 702
ChainResidue
CGLU97
CASP118
CLEU120
CPO4701
CMN703
CK704
CHOH801

site_idAD2
Number of Residues5
Detailsbinding site for residue MN C 703
ChainResidue
CASP118
CASP121
CGLU284
CPO4701
CMN702

site_idAD3
Number of Residues4
Detailsbinding site for residue K C 704
ChainResidue
CASP68
CGLU97
CPO4701
CMN702

site_idAD4
Number of Residues3
Detailsbinding site for residue CIT C 705
ChainResidue
ALYS52
CARG48
CLYS52

site_idAD5
Number of Residues10
Detailsbinding site for residue PO4 D 701
ChainResidue
DASP74
DGLU97
DASP118
DLEU120
DASP121
DSER123
DMN702
DMN703
DK704
DHOH803

site_idAD6
Number of Residues4
Detailsbinding site for residue MN D 702
ChainResidue
DK704
DASP74
DGLU98
DPO4701

site_idAD7
Number of Residues5
Detailsbinding site for residue MN D 703
ChainResidue
DGLU97
DASP118
DASP121
DGLU284
DPO4701

site_idAD8
Number of Residues7
Detailsbinding site for residue K D 704
ChainResidue
DASP74
DGLU97
DGLU98
DASP118
DLEU120
DPO4701
DMN702

site_idAD9
Number of Residues3
Detailsbinding site for residue CIT D 705
ChainResidue
BLYS52
DLYS44
DLYS52

Functional Information from PROSITE/UniProt
site_idPS00124
Number of Residues13
DetailsFBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEaaPMA
ChainResidueDetails
AGLY277-ALA289

246031

PDB entries from 2025-12-10

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