Structure of PDB 2zrx Chain D

Receptor sequence
>2zrxD (length=364) Species: 2286 (Saccharolobus shibatae) [Search protein sequence]
DIVNRKVEHVEIAAFENVDGLSSSTFLNDVILVHQGFPGISFSEINTKTK
FFRKEISVPVMVTGMTGGRNELGRINKIIAEVAEKFGIPMGVGSQRVAIE
KAEARESFAIVRKVAPTIPIIANLGMPQLVKGYGLKEFQDAIQMIEADAI
AVHLNPAQEVFQPEGEPEYQIYALEKLRDISKELSVPIIVKESGNGISME
TAKLLYSYGIKNFDTSGQGGTNWIAIEMIRDIRRGNWKAESAKNFLDWGV
PTAASIMEVRYSVPDSFLVGSGGIRSGLDAAKAIALGADIAGMALPVLKS
AIEGKESLEQFFRKIIFELKAAMMLTGSKDVDALKKTSIVILGKLKEWAE
YRGINLSIYEKVRK
3D structure
PDB2zrx New role of flavin as a general acid-base catalyst with no redox function in type 2 isopentenyl-diphosphate isomerase.
ChainD
Resolution3.0 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 FMN D T65 G66 M67 G95 S96 N125 H155 K193 S218 G222 T223 W225 G275 R277 A296 L297 T63 G64 M65 G93 S94 N123 H153 K191 S216 G220 T221 W223 G273 R275 A294 L295
BS02 DMA D R7 K8 S96 R98 H155 Q160 W225 R5 K6 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:2zrx, PDBe:2zrx, PDBj:2zrx
PDBsum2zrx
PubMed19158086
UniProtP61615|IDI2_SACSH Isopentenyl-diphosphate delta-isomerase (Gene Name=fni)

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