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1FXS

GDP-FUCOSE SYNTHETASE FROM ESCHERICHIA COLI COMPLEX WITH NADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0009226biological_processnucleotide-sugar biosynthetic process
A0009242biological_processcolanic acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016853molecular_functionisomerase activity
A0042351biological_process'de novo' GDP-L-fucose biosynthetic process
A0042803molecular_functionprotein homodimerization activity
A0050577molecular_functionGDP-L-fucose synthase activity
A0070401molecular_functionNADP+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAP A 350
ChainResidue
AARG12
AALA62
AALA63
AALA64
AVAL66
AILE86
ALEU105
AGLY106
ASER107
ASER108
ATYR136
AGLY13
ALYS140
APRO163
ATHR164
AASN165
ALEU166
AHOH385
AHOH423
AHOH428
AHOH429
AHOH430
AMET14
AVAL15
AARG36
ALEU39
AASN40
ALEU41
ALEU42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00956, ECO:0000269|PubMed:11021971
ChainResidueDetails
ATYR136

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00956, ECO:0000269|PubMed:11021971, ECO:0000269|PubMed:9817848, ECO:0000269|PubMed:9862812
ChainResidueDetails
AGLY10
AARG36
ALEU105
ALYS140
APRO163
AHIS179

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AARG187

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00956
ChainResidueDetails
ATRP202
AARG209
AASP278

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Important for catalytic activity
ChainResidueDetails
ASER107
ACYS109

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Lowers pKa of active site Tyr
ChainResidueDetails
ALYS140

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ACYS109
AHIS179
ATYR136
ALYS140

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ATYR136
ASER107
ALYS140

site_idMCSA1
Number of Residues6
DetailsM-CSA 227
ChainResidueDetails
ASER107electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity, increase basicity, proton acceptor, proton donor
ASER108electrostatic stabiliser, hydrogen bond donor
ACYS109electrostatic stabiliser, hydrogen bond donor, proton acceptor
ATYR136electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
ALYS140electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity
AHIS179hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-07-17

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