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1KET

The crystal structure of dTDP-D-glucose 4,6-dehydratase (RmlB) from Streptococcus suis with thymidine diphosphate bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0008460molecular_functiondTDP-glucose 4,6-dehydratase activity
A0009103biological_processlipopolysaccharide biosynthetic process
A0009225biological_processnucleotide-sugar metabolic process
A0016829molecular_functionlyase activity
A0019305biological_processdTDP-rhamnose biosynthetic process
A0045226biological_processextracellular polysaccharide biosynthetic process
B0008460molecular_functiondTDP-glucose 4,6-dehydratase activity
B0009103biological_processlipopolysaccharide biosynthetic process
B0009225biological_processnucleotide-sugar metabolic process
B0016829molecular_functionlyase activity
B0019305biological_processdTDP-rhamnose biosynthetic process
B0045226biological_processextracellular polysaccharide biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE TYD A 2573
ChainResidue
AHIS87
ATYR218
AARG225
AASN260
AARG284
AHIS287
ATYR340
AHOH2615
AHOH2632
AHOH2635
AHOH2811
AASN88
AGLU127
AASN190
AGLU199
APHE201
AARG204
AGLN205
ALYS216

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE TYD B 2574
ChainResidue
BHIS87
BASN88
BGLU127
BASN190
BGLU199
BPHE201
BARG204
BGLN205
BLYS216
BLEU217
BTYR218
BARG225
BASN260
BARG284
BHIS287
BTYR340
BHOH2626
BHOH2657
BHOH2687
BHOH2722

site_idAC3
Number of Residues35
DetailsBINDING SITE FOR RESIDUE NAD A 1400
ChainResidue
AALA13
AGLY14
APHE15
AILE16
AASP37
ALYS38
ALEU39
ATHR40
AALA42
AGLY43
AGLY61
AASP62
AILE63
ATYR82
AALA84
ASER86
ATHR101
AVAL123
ASER124
ATYR161
ALYS165
ACYS188
ASER189
AASN190
AASN191
AHOH2575
AHOH2578
AHOH2579
AHOH2583
AHOH2587
AHOH2592
AHOH2599
AHOH2606
AHOH2660
AHOH2784

site_idAC4
Number of Residues34
DetailsBINDING SITE FOR RESIDUE NAD B 1500
ChainResidue
BHOH2578
BHOH2580
BHOH2581
BHOH2583
BHOH2587
BHOH2594
BHOH2596
BHOH2635
BHOH2669
BALA13
BGLY14
BPHE15
BILE16
BASP37
BLYS38
BLEU39
BTHR40
BALA42
BGLY43
BGLY61
BASP62
BILE63
BTYR82
BALA84
BSER86
BTHR101
BVAL123
BSER124
BTHR125
BTYR161
BLYS165
BCYS188
BSER189
BASN191

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P27830
ChainResidueDetails
AASP126
BASP126

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P27830
ChainResidueDetails
AGLU127
BGLU127

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:11796113, ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET
ChainResidueDetails
ATYR161
BTYR161

site_idSWS_FT_FI4
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:11796113, ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET
ChainResidueDetails
APHE15
BASP62
BTYR82
BTHR101
BASN191
BLYS200
AASP37
AASP62
ATYR82
ATHR101
AASN191
ALYS200
BPHE15
BASP37

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P26391
ChainResidueDetails
ASER86
BSER86

site_idSWS_FT_FI6
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:11796113, ECO:0007744|PDB:1KET
ChainResidueDetails
AASN88
BASN260
AASN190
ALYS216
AARG225
AASN260
BASN88
BASN190
BLYS216
BARG225

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11796113, ECO:0007744|PDB:1KEP
ChainResidueDetails
ATHR125
BTHR125

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:11796113, ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET
ChainResidueDetails
ATYR161
BTYR161

site_idSWS_FT_FI9
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:11796113, ECO:0007744|PDB:1KET
ChainResidueDetails
AASP283
BASP283

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ATYR161
ALYS165
ATHR125

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
BTYR161
BLYS165
BTHR125

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ATYR161
AGLU127
ATHR125
ALYS165

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
BTYR161
BGLU127
BTHR125
BLYS165

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ATYR161
ALYS165

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
BTYR161
BLYS165

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PDB entries from 2024-10-30

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