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1DZR

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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AARG60
AHIS63
ALYS73
AHIS120
ATYR133
ATYR139
AHOH2153

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 301
ChainResidue
BHIS120
BTYR133
BTYR139
BHIS63
BLYS73

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AASN103
AARG110
AHOH2154
AHOH2155

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BASN103
BARG110
BHOH2126

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 201
ChainResidue
AMET2
APRO17
AGLU29
ASER30
ATYR31
AASN32
APHE36
AGLN111

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 202
ChainResidue
AMET1
AMET2
ALYS18
AHOH2145
BMET1

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 203
ChainResidue
AGLY21
AGLY25
AHOH2146

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 204
ChainResidue
ATRP99
AGLY101
AHOH2148
AHOH2149
AHOH2150

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 205
ChainResidue
AARG60
AHIS63
ASER167
ALYS169
AASP170
AHOH2151
AHOH2152
BARG24

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
AARG60
ALYS73
AHIS120
BARG60
BLYS73
BHIS120

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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 10802738
ChainResidueDetails
AASP170
AHIS63

site_idCSA2
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 10802738
ChainResidueDetails
BASP170
BHIS63

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PDB entries from 2024-10-09

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