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7JLM

Crystal structure of Bacillus subtilis UppS in complex with MAC-0547630

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004659molecular_functionprenyltransferase activity
A0005829cellular_componentcytosol
A0008834molecular_functiondi-trans,poly-cis-undecaprenyl-diphosphate synthase activity
A0016094biological_processpolyprenol biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0030145molecular_functionmanganese ion binding
A0045547molecular_functiondehydrodolichyl diphosphate synthase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004659molecular_functionprenyltransferase activity
B0005829cellular_componentcytosol
B0008834molecular_functiondi-trans,poly-cis-undecaprenyl-diphosphate synthase activity
B0016094biological_processpolyprenol biosynthetic process
B0016740molecular_functiontransferase activity
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0030145molecular_functionmanganese ion binding
B0045547molecular_functiondehydrodolichyl diphosphate synthase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CIT A 301
ChainResidue
AASN88
ALYS90
AARG208
AARG214
ASER216
AHOH435

site_idAC2
Number of Residues14
Detailsbinding site for residue V07 A 302
ChainResidue
AGLY60
AMET61
AALA83
ALEU99
ALEU102
APRO103
APHE106
AILE123
AILE138
APHE155
ALEU157
AMET39
AASN42
AHIS57

site_idAC3
Number of Residues7
Detailsbinding site for residue CIT B 301
ChainResidue
BMET39
BASP40
BGLY41
BASN42
BGLY43
BARG44
BHIS57

site_idAC4
Number of Residues14
Detailsbinding site for residue V07 B 302
ChainResidue
BMET39
BASN42
BHIS57
BMET61
BVAL64
BLEU99
BMET100
BLEU102
BPRO103
BPHE106
BLEU107
BILE138
BPHE155
BLEU157

Functional Information from PROSITE/UniProt
site_idPS01066
Number of Residues18
DetailsUPP_SYNTHASE Undecaprenyl pyrophosphate synthase family signature. ELLIRTSGeiRlSnFMLW
ChainResidueDetails
AGLU204-TRP221

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01139
ChainResidueDetails
AASP40
BASP40

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01139
ChainResidueDetails
AASN88
BASN88

site_idSWS_FT_FI3
Number of Residues22
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01139
ChainResidueDetails
AASP40
AARG214
AGLU227
BASP40
BGLY41
BTRP45
BARG53
BHIS57
BSER85
BTRP89
BARG91
AGLY41
BARG208
BARG214
BGLU227
ATRP45
AARG53
AHIS57
ASER85
ATRP89
AARG91
AARG208

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PDB entries from 2024-08-28

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