Structure of PDB 1q54 Chain A

Receptor sequence

>1q54A (length=176) Species: 562 (Escherichia coli)

EHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRAL
SKKAWPGVWTNSVAGHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFR
YRATDPSGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDA
TPWAFSPWMVMQATNREARKRLSAFT

3D structure

• PDB: 1q54 Structure and mechanism of action of isopentenylpyrophosphate-dimethylallylpyrophosphate isomerase.
• Chain: A
• Resolution: 1.93 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H25 H32 A67 H69 E87 Y104 E114 E116 W161
• Catalytic site (residue number reindexed from 1): H22 H29 A64 H66 E84 Y101 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	A	H25 H32 H69 E114 E116	H22 H29 H66 E111 E113
BS02	MG	A	A67 E87	A64 E84
BS03	BHI	A	R51 K55 A67 G68 R83 E87 E114 E116 W161	R48 K52 A64 G65 R80 E84 E111 E113 W158	MOAD: Ki=1.4uM PDBbind-CN: -logKd/Ki=5.85,Ki=1.4uM

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

External links

• PDB: RCSB:1q54, PDBe:1q54, PDBj:1q54
• PDBsum: 1q54
• PubMed: 12630859
• UniProt: Q46822|IDI_ECOLI Isopentenyl-diphosphate Delta-isomerase (Gene Name=idi)