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3SR7

Crystal structure of S. mutans isopentenyl pyrophosphate isomerase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004452molecular_functionisopentenyl-diphosphate delta-isomerase activity
A0005737cellular_componentcytoplasm
A0008299biological_processisoprenoid biosynthetic process
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016853molecular_functionisomerase activity
A0046872molecular_functionmetal ion binding
A0070402molecular_functionNADPH binding
B0000287molecular_functionmagnesium ion binding
B0004452molecular_functionisopentenyl-diphosphate delta-isomerase activity
B0005737cellular_componentcytoplasm
B0008299biological_processisoprenoid biosynthetic process
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0016853molecular_functionisomerase activity
B0046872molecular_functionmetal ion binding
B0070402molecular_functionNADPH binding
C0000287molecular_functionmagnesium ion binding
C0004452molecular_functionisopentenyl-diphosphate delta-isomerase activity
C0005737cellular_componentcytoplasm
C0008299biological_processisoprenoid biosynthetic process
C0010181molecular_functionFMN binding
C0016491molecular_functionoxidoreductase activity
C0016853molecular_functionisomerase activity
C0046872molecular_functionmetal ion binding
C0070402molecular_functionNADPH binding
D0000287molecular_functionmagnesium ion binding
D0004452molecular_functionisopentenyl-diphosphate delta-isomerase activity
D0005737cellular_componentcytoplasm
D0008299biological_processisoprenoid biosynthetic process
D0010181molecular_functionFMN binding
D0016491molecular_functionoxidoreductase activity
D0016853molecular_functionisomerase activity
D0046872molecular_functionmetal ion binding
D0070402molecular_functionNADPH binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 C 332
ChainResidue
AARG326
AARG330
BARG326
BARG330
CARG326
CARG330
DARG326
DARG330

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues44
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00354
ChainResidueDetails
AARG4
AGLY252
ASER273
BARG4
BALA59
BSER89
BASN116
BGLN146
BGLU147
BLYS178
BSER203
AALA59
BTHR208
BGLY252
BSER273
CARG4
CALA59
CSER89
CASN116
CGLN146
CGLU147
CLYS178
ASER89
CSER203
CTHR208
CGLY252
CSER273
DARG4
DALA59
DSER89
DASN116
DGLN146
DGLU147
AASN116
DLYS178
DSER203
DTHR208
DGLY252
DSER273
AGLN146
AGLU147
ALYS178
ASER203
ATHR208

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PDB entries from 2024-08-21

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