Structure of PDB 2zrz Chain C

Receptor sequence
>2zrzC (length=364) Species: 2286 (Saccharolobus shibatae) [Search protein sequence]
DIVNRKVEHVEIAAFENVDGLSSSTFLNDVILVHQGFPGISFSEINTKTK
FFRKEISVPVMVTGMTGGRNELGRINKIIAEVAEKFGIPMGVGSQRVAIE
KAEARESFAIVRKVAPTIPIIANLGMPQLVKGYGLKEFQDAIQMIEADAI
AVHLNPAQEVFQPEGEPEYQIYALEKLRDISKELSVPIIVKESGNGISME
TAKLLYSYGIKNFDTSGQGGTNWIAIEMIRDIRRGNWKAESAKNFLDWGV
PTAASIMEVRYSVPDSFLVGSGGIRSGLDAAKAIALGADIAGMALPVLKS
AIEGKESLEQFFRKIIFELKAAMMLTGSKDVDALKKTSIVILGKLKEWAE
YRGINLSIYEKVRK
3D structure
PDB2zrz New role of flavin as a general acid-base catalyst with no redox function in type 2 isopentenyl-diphosphate isomerase.
ChainC
Resolution2.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 5.3.3.2: isopentenyl-diphosphate Delta-isomerase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FNR C T65 G66 M67 G95 S96 N125 H155 K193 S218 T223 W225 R277 A296 L297 T63 G64 M65 G93 S94 N123 H153 K191 S216 T221 W223 R275 A294 L295
BS02 DMA C R7 K8 H11 S96 R98 H155 Q160 W225 R5 K6 H9 S94 R96 H153 Q158 W223
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004452 isopentenyl-diphosphate delta-isomerase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
GO:0070402 NADPH binding
Biological Process
GO:0008299 isoprenoid biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2zrz, PDBe:2zrz, PDBj:2zrz
PDBsum2zrz
PubMed19158086
UniProtP61615|IDI2_SACSH Isopentenyl-diphosphate delta-isomerase (Gene Name=fni)

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