Structure of PDB 2g74 Chain B

Receptor sequence
>2g74B (length=180) Species: 562 (Escherichia coli) [Search protein sequence]
EHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRAL
SKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFR
FRATDPSGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDA
TPWAFSPWMVMQATNREARKRLSAFTQLKL
3D structure
PDB2g74 Structural role for Tyr-104 in Escherichia coli isopentenyl-diphosphate isomerase: site-directed mutagenesis, enzymology, and protein crystallography.
ChainB
Resolution1.96 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H25 H32 C67 H69 E87 F104 E114 E116 W161
Catalytic site (residue number reindexed from 1) H22 H29 C64 H66 E84 F101 E111 E113 W158
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 MN B H25 H32 H69 E114 E116 H22 H29 H66 E111 E113
BS02 MG B C67 R83 E87 C64 R80 E84
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004452 isopentenyl-diphosphate delta-isomerase activity
GO:0008270 zinc ion binding
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0006974 DNA damage response
GO:0008299 isoprenoid biosynthetic process
GO:0050992 dimethylallyl diphosphate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2g74, PDBe:2g74, PDBj:2g74
PDBsum2g74
PubMed16617181
UniProtQ46822|IDI_ECOLI Isopentenyl-diphosphate Delta-isomerase (Gene Name=idi)

[Back to BioLiP]