Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4E5Y

Structure of human FX protein, the key enzyme in the biosynthesis of GDP-L-fucose

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0007159biological_processleukocyte cell-cell adhesion
A0009055molecular_functionelectron transfer activity
A0009226biological_processnucleotide-sugar biosynthetic process
A0010595biological_processpositive regulation of endothelial cell migration
A0016491molecular_functionoxidoreductase activity
A0016853molecular_functionisomerase activity
A0019673biological_processGDP-mannose metabolic process
A0042351biological_process'de novo' GDP-L-fucose biosynthetic process
A0042356molecular_functionGDP-4-dehydro-D-rhamnose reductase activity
A0042802molecular_functionidentical protein binding
A0047918molecular_functionGDP-mannose 3,5-epimerase activity
A0050577molecular_functionGDP-L-fucose synthase activity
A0070062cellular_componentextracellular exosome
A1904906biological_processpositive regulation of endothelial cell-matrix adhesion via fibronectin
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0007159biological_processleukocyte cell-cell adhesion
B0009055molecular_functionelectron transfer activity
B0009226biological_processnucleotide-sugar biosynthetic process
B0010595biological_processpositive regulation of endothelial cell migration
B0016491molecular_functionoxidoreductase activity
B0016853molecular_functionisomerase activity
B0019673biological_processGDP-mannose metabolic process
B0042351biological_process'de novo' GDP-L-fucose biosynthetic process
B0042356molecular_functionGDP-4-dehydro-D-rhamnose reductase activity
B0042802molecular_functionidentical protein binding
B0047918molecular_functionGDP-mannose 3,5-epimerase activity
B0050577molecular_functionGDP-L-fucose synthase activity
B0070062cellular_componentextracellular exosome
B1904906biological_processpositive regulation of endothelial cell-matrix adhesion via fibronectin
C0005515molecular_functionprotein binding
C0005829cellular_componentcytosol
C0007159biological_processleukocyte cell-cell adhesion
C0009055molecular_functionelectron transfer activity
C0009226biological_processnucleotide-sugar biosynthetic process
C0010595biological_processpositive regulation of endothelial cell migration
C0016491molecular_functionoxidoreductase activity
C0016853molecular_functionisomerase activity
C0019673biological_processGDP-mannose metabolic process
C0042351biological_process'de novo' GDP-L-fucose biosynthetic process
C0042356molecular_functionGDP-4-dehydro-D-rhamnose reductase activity
C0042802molecular_functionidentical protein binding
C0047918molecular_functionGDP-mannose 3,5-epimerase activity
C0050577molecular_functionGDP-L-fucose synthase activity
C0070062cellular_componentextracellular exosome
C1904906biological_processpositive regulation of endothelial cell-matrix adhesion via fibronectin
D0005515molecular_functionprotein binding
D0005829cellular_componentcytosol
D0007159biological_processleukocyte cell-cell adhesion
D0009055molecular_functionelectron transfer activity
D0009226biological_processnucleotide-sugar biosynthetic process
D0010595biological_processpositive regulation of endothelial cell migration
D0016491molecular_functionoxidoreductase activity
D0016853molecular_functionisomerase activity
D0019673biological_processGDP-mannose metabolic process
D0042351biological_process'de novo' GDP-L-fucose biosynthetic process
D0042356molecular_functionGDP-4-dehydro-D-rhamnose reductase activity
D0042802molecular_functionidentical protein binding
D0047918molecular_functionGDP-mannose 3,5-epimerase activity
D0050577molecular_functionGDP-L-fucose synthase activity
D0070062cellular_componentextracellular exosome
D1904906biological_processpositive regulation of endothelial cell-matrix adhesion via fibronectin
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NDP A 401
ChainResidue
AGLY14
ALEU48
ALEU69
AALA70
AALA71
ACYS112
ALEU113
ASER114
ATYR143
ALYS147
APRO170
ASER16
ATHR171
AVAL173
AARG320
AGLY17
ALEU18
AVAL19
ASER42
ASER43
AALA46
AASP47

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NDP B 401
ChainResidue
BGLY14
BSER16
BGLY17
BLEU18
BVAL19
BSER42
BSER43
BLYS44
BALA46
BASP47
BLEU48
BLEU69
BALA70
BALA71
BVAL73
BCYS112
BLEU113
BSER114
BTYR143
BLYS147
BPRO170
BTHR171
BVAL173
BARG320

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NDP C 401
ChainResidue
CGLY14
CSER16
CGLY17
CLEU18
CVAL19
CSER42
CSER43
CALA46
CASP47
CLEU48
CLEU69
CALA70
CALA71
CVAL73
CMET93
CCYS112
CLEU113
CSER114
CTYR143
CLYS147
CTHR171
CVAL173
CHIS186
CARG320

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NDP D 401
ChainResidue
DGLY14
DSER16
DGLY17
DLEU18
DVAL19
DSER42
DSER43
DALA46
DASP47
DLEU48
DLEU69
DALA70
DALA71
DCYS112
DLEU113
DSER114
DTYR143
DLYS147
DPRO170
DTHR171
DASN172
DVAL173
DARG320
DHOH502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250
ChainResidueDetails
ATYR143
BTYR143
CTYR143
DTYR143

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:23774504, ECO:0000269|Ref.9
ChainResidueDetails
AGLY14
DGLY14
DLYS147
DPRO170
ALYS147
APRO170
BGLY14
BLYS147
BPRO170
CGLY14
CLYS147
CPRO170

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|Ref.9
ChainResidueDetails
AHIS186
BHIS186
CHIS186
DHIS186

site_idSWS_FT_FI4
Number of Residues16
DetailsBINDING: BINDING => ECO:0000305|Ref.9
ChainResidueDetails
ALYS194
CTRP208
CARG215
CASP277
DLYS194
DTRP208
DARG215
DASP277
ATRP208
AARG215
AASP277
BLYS194
BTRP208
BARG215
BASP277
CLYS194

site_idSWS_FT_FI5
Number of Residues8
DetailsSITE: Important for catalytic activity => ECO:0000250
ChainResidueDetails
ASER114
ACYS116
BSER114
BCYS116
CSER114
CCYS116
DSER114
DCYS116

site_idSWS_FT_FI6
Number of Residues4
DetailsSITE: Lowers pKa of active site Tyr => ECO:0000250
ChainResidueDetails
ALYS147
BLYS147
CLYS147
DLYS147

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon