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1E7Q

GDP 4-keto-6-deoxy-D-mannose epimerase reductase S107A

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 Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1319
ChainResidue
AARG5
AVAL32
AARG34
AGLU54
AHOH2306

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A1320
ChainResidue
AHIS11
AARG12
AARG20

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A1321
ChainResidue
AGLN237
APRO238
AVAL271
AHOH2224
AHOH2307
AASP198

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A1322
ChainResidue
AARG152
APRO238
AARG254
AVAL270
AVAL271
APHE272
AHOH2236
AHOH2308
AHOH2309
AHOH2310

site_idAC5
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAP A1317
ChainResidue
AGLY10
AGLY13
AMET14
AVAL15
AARG36
ALEU39
AASN40
ALEU41
ALEU42
AALA62
AALA63
AALA64
AVAL66
AILE86
ALEU105
AGLY106
ATYR136
ALYS140
APRO163
ALEU166
AHOH2012
AHOH2092
AHOH2296
AHOH2297
AHOH2299
AHOH2300
AHOH2301
AHOH2302
AHOH2303

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE UVW A1318
ChainResidue
AGLY68
AILE69
AVAL70
AALA71
ASER178
ALYS262
AHOH2304
AHOH2305

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRS A1323
ChainResidue
AARG21
AHIS170
ATRP311
AHOH2311
AHOH2312
AHOH2313
AHOH2314

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
AALA107
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
Detailsa catalytic site defined by CSA, PubMed 9862812, 11021971
ChainResidueDetails
ACYS109
AHIS179
ATYR136
ALYS140

site_idCSA2
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 9862812, 11021971
ChainResidueDetails
ATYR136
AALA107
ALYS140

site_idMCSA1
Number of Residues6
DetailsM-CSA 227
ChainResidueDetails
AALA107electrostatic 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 2024-10-09

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