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3VKJ

Crystal structure of Sulfolobus shibatae isopentenyl diphosphate isomerase, octameric form

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 Residues20
DetailsBINDING SITE FOR RESIDUE FNR A 401
ChainResidue
ATHR65
AGLY222
ATHR223
ATRP225
AGLY275
AARG277
AALA296
ALEU297
AHOH505
AHOH525
AHOH577
AGLY66
AHOH587
AMET67
AGLY95
ASER96
AASN125
AHIS155
ALYS193
ASER218

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FNR B 401
ChainResidue
BTHR65
BGLY66
BMET67
BGLY95
BSER96
BASN125
BHIS155
BLYS193
BSER218
BGLY222
BTHR223
BTRP225
BGLY275
BARG277
BMET295
BALA296
BLEU297
BHOH501
BHOH508
BHOH511
BHOH569
BHOH629

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FNR C 401
ChainResidue
CTHR65
CGLY66
CMET67
CGLY95
CSER96
CASN125
CHIS155
CLYS193
CSER218
CGLY222
CTHR223
CTRP225
CGLY275
CARG277
CMET295
CALA296
CLEU297
CHOH501
CHOH502
CHOH526
CHOH568
CHOH697

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FNR D 401
ChainResidue
DTHR65
DGLY66
DMET67
DGLY95
DSER96
DASN125
DHIS155
DLYS193
DSER218
DGLY222
DTHR223
DTRP225
DGLY275
DARG277
DALA296
DLEU297
DHOH502
DHOH503
DHOH507
DHOH654
DHOH672

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AARG7
AGLN160
BARG7
BGLN160
CARG7
CGLN160
DARG7
DGLN160

site_idSWS_FT_FI2
Number of Residues40
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00354, ECO:0000269|PubMed:19158086, ECO:0000269|PubMed:22158896
ChainResidueDetails
ATHR65
AALA296
BTHR65
BGLY66
BSER96
BASN125
BGLU161
BLYS193
BSER218
BTHR223
BGLY275
AGLY66
BALA296
CTHR65
CGLY66
CSER96
CASN125
CGLU161
CLYS193
CSER218
CTHR223
CGLY275
ASER96
CALA296
DTHR65
DGLY66
DSER96
DASN125
DGLU161
DLYS193
DSER218
DTHR223
DGLY275
AASN125
DALA296
AGLU161
ALYS193
ASER218
ATHR223
AGLY275

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PDB entries from 2024-07-03

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