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3PKQ

Q83D Variant of S. Enterica RmlA with dGTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0008879molecular_functionglucose-1-phosphate thymidylyltransferase activity
A0009058biological_processbiosynthetic process
A0009103biological_processlipopolysaccharide biosynthetic process
A0009243biological_processO antigen biosynthetic process
A0016779molecular_functionnucleotidyltransferase activity
A0019305biological_processdTDP-rhamnose biosynthetic process
A0045226biological_processextracellular polysaccharide biosynthetic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0008879molecular_functionglucose-1-phosphate thymidylyltransferase activity
B0009058biological_processbiosynthetic process
B0009103biological_processlipopolysaccharide biosynthetic process
B0009243biological_processO antigen biosynthetic process
B0016779molecular_functionnucleotidyltransferase activity
B0019305biological_processdTDP-rhamnose biosynthetic process
B0045226biological_processextracellular polysaccharide biosynthetic process
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0008879molecular_functionglucose-1-phosphate thymidylyltransferase activity
C0009058biological_processbiosynthetic process
C0009103biological_processlipopolysaccharide biosynthetic process
C0009243biological_processO antigen biosynthetic process
C0016779molecular_functionnucleotidyltransferase activity
C0019305biological_processdTDP-rhamnose biosynthetic process
C0045226biological_processextracellular polysaccharide biosynthetic process
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0008879molecular_functionglucose-1-phosphate thymidylyltransferase activity
D0009058biological_processbiosynthetic process
D0009103biological_processlipopolysaccharide biosynthetic process
D0009243biological_processO antigen biosynthetic process
D0016779molecular_functionnucleotidyltransferase activity
D0019305biological_processdTDP-rhamnose biosynthetic process
D0045226biological_processextracellular polysaccharide biosynthetic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE DGT A 500
ChainResidue
ALEU9
AILE55
AASP83
ASER85
APRO86
AGLY110
AASP111
AHOH356
AHOH375
AMG501
AGLY11
AGLY12
ASER13
AGLY14
ATHR15
AARG16
ALYS26
AGLN27

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AASP111
AASP226
ADGT500

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PEG A 293
ChainResidue
ALYS5
AASP104
AALA126
AVAL127
AGLY132
APHE178
ATYR179
AASP180
AHOH318

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 294
ChainResidue
AHIS230
ALEU233
AILE234
ASER237
BTYR32
BSER237
BHOH336

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE DGT B 500
ChainResidue
BLEU9
BGLY11
BGLY12
BSER13
BGLY14
BTHR15
BARG16
BLYS26
BGLN27
BILE55
BASP83
BPRO86
BGLY110
BASP111
BHOH311
BMG501
BMG502

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 501
ChainResidue
BLYS26
BASP111
BASP226
BDGT500

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG B 502
ChainResidue
BDGT500

site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE DGT C 500
ChainResidue
CLEU9
CGLY11
CGLY12
CSER13
CGLY14
CTHR15
CARG16
CLYS26
CGLN27
CILE55
CASP83
CSER85
CGLY110
CASP111
CHOH302
CMG501

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 501
ChainResidue
CLYS26
CASP111
CASP226
CDGT500

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG C 293
ChainResidue
CTYR32
CSER237
DHIS230
DLEU233
DILE234
DSER237

site_idBC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE DGT D 500
ChainResidue
DHOH298
DMG502
DLEU9
DGLY11
DGLY12
DSER13
DGLY14
DTHR15
DARG16
DLYS26
DGLN27
DILE55
DASP83
DSER85
DGLY110
DASP111

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG D 502
ChainResidue
DDGT500

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P61887
ChainResidueDetails
AASP111
AASP226
BASP111
BASP226
CASP111
CASP226
DASP111
DASP226

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PDB entries from 2024-08-28

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