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4B8W

Crystal structure of human GDP-L-fucose synthase with bound NADP and GDP, tetragonal crystal form

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
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAP A 900
ChainResidue
AGLY14
ALEU48
ALEU69
AALA70
AALA71
AMET93
ACYS112
ALEU113
ATYR143
ALYS147
ATHR171
ASER16
AVAL173
AHIS186
AARG320
AGLY17
ALEU18
AVAL19
ASER42
ASER43
AALA46
AASP47

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GDP A 901
ChainResidue
AGLY75
ALEU76
APHE77
AASN172
AGLY185
AHIS186
AVAL187
AVAL207
ATRP208
APRO213
AARG215
AILE252
ASER276
AASP277
ALYS282
AHOH2009

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAP B 900
ChainResidue
BGLY14
BSER16
BGLY17
BLEU18
BVAL19
BSER42
BSER43
BALA46
BASP47
BLEU48
BLEU69
BALA70
BALA71
BCYS112
BLEU113
BTYR143
BLYS147
BTHR171
BVAL173
BHIS186
BHIS266

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GDP B 901
ChainResidue
BASN172
BGLY185
BHIS186
BVAL187
BVAL207
BTRP208
BARG215
BSER276
BASP277
BLYS282

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250
ChainResidueDetails
ATYR143
BTYR143

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:23774504, ECO:0000269|Ref.9
ChainResidueDetails
AGLY14
ALYS147
APRO170
BGLY14
BLYS147
BPRO170

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.9
ChainResidueDetails
AHIS186
BHIS186

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|Ref.9
ChainResidueDetails
ALYS194
ATRP208
AARG215
AASP277
BLYS194
BTRP208
BARG215
BASP277

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Important for catalytic activity => ECO:0000250
ChainResidueDetails
ASER114
ACYS116
BSER114
BCYS116

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Lowers pKa of active site Tyr => ECO:0000250
ChainResidueDetails
ALYS147
BLYS147

227111

PDB entries from 2024-11-06

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