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1DZT

RMLC FROM SALMONELLA TYPHIMURIUM

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0008830molecular_functiondTDP-4-dehydrorhamnose 3,5-epimerase activity
A0009103biological_processlipopolysaccharide biosynthetic process
A0009243biological_processO antigen biosynthetic process
A0016853molecular_functionisomerase activity
A0019305biological_processdTDP-rhamnose biosynthetic process
A0045226biological_processextracellular polysaccharide biosynthetic process
B0005829cellular_componentcytosol
B0008830molecular_functiondTDP-4-dehydrorhamnose 3,5-epimerase activity
B0009103biological_processlipopolysaccharide biosynthetic process
B0009243biological_processO antigen biosynthetic process
B0016853molecular_functionisomerase activity
B0019305biological_processdTDP-rhamnose biosynthetic process
B0045226biological_processextracellular polysaccharide biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AARG60
AHIS63
ALYS73
AHIS120
ATYR133
AHOH2165

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BTYR133
BATY1000
BHIS63
BLYS73
BHIS120

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE TPE A 1000
ChainResidue
ALYS18
AGLN48
AARG60
ATYR139
ASER167
ALYS169
AHOH2145
AHOH2146
AHOH3001
AHOH3002
BPHE20
BARG24
BPHE27
BGLU29
BTYR139
BPRO141

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATY B 1000
ChainResidue
APHE27
AGLU29
APRO141
ASER142
AHOH3004
BGLN48
BASN50
BHIS63
BTYR133
BTYR139
BGLU144
BSER167
BLYS169
BSO4302
BHOH2050
BHOH2117
BHOH3005
BHOH3006
BHOH3007

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 201
ChainResidue
BTRP99
BGLY101
BHOH2147

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 202
ChainResidue
APHE20
AGLY25
ASER142

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 203
ChainResidue
ATRP99
AVAL100
AGLY101

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 204
ChainResidue
AGLU81
ALEU125

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:10802738, ECO:0000269|PubMed:17046787, ECO:0007744|PDB:1DZR, ECO:0007744|PDB:1DZT
ChainResidueDetails
AHIS63
BHIS63

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:10802738, ECO:0000269|PubMed:17046787, ECO:0007744|PDB:1DZT
ChainResidueDetails
ATYR133
BTYR133

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9HU21
ChainResidueDetails
AARG24
AGLU144
BARG24
BGLU144

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10802738, ECO:0007744|PDB:1DZT
ChainResidueDetails
AGLU29
ALYS169
BGLU29
BLYS169

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:10802738, ECO:0007744|PDB:1DZT
ChainResidueDetails
AGLN48
BGLN48

site_idSWS_FT_FI6
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10802738, ECO:0007744|PDB:1DZR, ECO:0007744|PDB:1DZT
ChainResidueDetails
AHIS120
BARG60
BLYS73
BHIS120
AARG60
ALYS73

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Participates in a stacking interaction with the thymidine ring of dTDP-4-oxo-6-deoxyglucose => ECO:0000250|UniProtKB:Q5SFD1
ChainResidueDetails
ATYR139
BTYR139

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PDB entries from 2024-06-12

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