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2ZRV

Crystal structure of Sulfolobus shibatae isopentenyl diphosphate isomerase in complex with reduced FMN.

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 669
ChainResidue
ATHR65
AGLY222
ATHR223
ATRP225
AGLY275
AARG277
AALA296
ALEU297
AHOH672
AHOH689
AHOH706
AGLY66
AHOH782
AMET67
AGLY95
ASER96
AASN125
AHIS155
ALYS193
ASER218

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FNR B 669
ChainResidue
BTHR65
BGLY66
BMET67
BGLY95
BSER96
BASN125
BHIS155
BLYS193
BSER218
BGLY222
BTHR223
BTRP225
BGLY275
BARG277
BMET295
BALA296
BLEU297
BHOH670
BHOH679
BHOH683
BHOH791

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FNR C 669
ChainResidue
CTHR65
CGLY66
CMET67
CGLY95
CSER96
CASN125
CHIS155
CLYS193
CSER218
CGLY222
CTHR223
CTRP225
CGLY274
CGLY275
CARG277
CALA296
CLEU297
CHOH670
CHOH671
CHOH700
CHOH800

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FNR D 669
ChainResidue
DTHR65
DGLY66
DMET67
DGLY95
DSER96
DASN125
DHIS155
DLYS193
DGLU194
DSER218
DGLY222
DTHR223
DTRP225
DGLY275
DARG277
DALA296
DLEU297
DHOH702
DHOH703
DHOH710

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues48
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00354","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19158086","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22158896","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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