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1VCG

Crystal Structure of IPP isomerase at P43212

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
B0000166molecular_functionnucleotide 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
C0000166molecular_functionnucleotide 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
D0000166molecular_functionnucleotide 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 Residues17
DetailsBINDING SITE FOR RESIDUE FMN A 501
ChainResidue
AALA65
AGLY190
ATHR217
ATRP219
AGLY263
AGLY264
ATYR266
AALA285
AARG286
AMSE66
ATHR67
AGLY94
ASER95
AASN123
AHIS152
ALYS187
AVAL189

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE FMN B 502
ChainResidue
BALA65
BMSE66
BTHR67
BGLY94
BSER95
BASN123
BHIS152
BLYS187
BVAL189
BGLY190
BTHR217
BTRP219
BGLY263
BGLY264
BTYR266
BALA285
BARG286

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE FMN C 503
ChainResidue
CALA65
CMSE66
CTHR67
CGLY94
CSER95
CASN123
CHIS152
CLYS187
CVAL189
CGLY190
CTHR217
CTRP219
CGLY263
CGLY264
CTYR266
CALA285
CARG286

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FMN D 504
ChainResidue
DALA65
DMSE66
DTHR67
DSER95
DASN123
DHIS152
DLYS187
DVAL189
DGLY190
DTHR217
DTRP219
DGLY263
DGLY264
DTYR266
DALA285
DARG286

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00354
ChainResidueDetails
AARG6
DARG6
DGLN157
DGLU158
AGLN157
AGLU158
BARG6
BGLN157
BGLU158
CARG6
CGLN157
CGLU158

site_idSWS_FT_FI2
Number of Residues28
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00354, ECO:0000269|Ref.3, ECO:0000269|Ref.4
ChainResidueDetails
AALA65
BASN123
BLYS187
BTHR217
BGLY264
BALA285
CALA65
CSER95
CASN123
CLYS187
CTHR217
ASER95
CGLY264
CALA285
DALA65
DSER95
DASN123
DLYS187
DTHR217
DGLY264
DALA285
AASN123
ALYS187
ATHR217
AGLY264
AALA285
BALA65
BSER95

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PDB entries from 2024-06-19

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