Structure of PDB 2j66 Chain A

Receptor sequence

>2j66A (length=390) Species: 1397 (Niallia circulans)

DQAEITALTKRFETPFYLYDGDFIEAHYRQLRSRTNPAIQFYLSLKANNN
IHLAKLFRQWGLGVEVASAGELALARHAGFSAENIIFSGPGKKRSELEIA
VQSGIYCIIAESVEELFYIEELAEKENKTARVAIRINPDKSFTAIKMGGV
PRQFGMDESMLDAVMDAVRSLQFTKFIGIHVYTGTQNLNTDSIIESMKYT
VDLGRNIYERYGIVCECINLGGGFGVPYFEKALDIGKITRTVSDYVQEAR
DTRFPQTTFIIESGRYLLAQAAVYVTEVLYRKASKGEVFVIVDGGMHHHA
ASPMEYIPLEKVTIAGPLCTPEDCLGKDVHVPALYPGDLVCVLNSGAYGL
SFSPVHFLGHPTPIEILKRNGSYELIRRKGTADDIVATQL

3D structure

• PDB: 2j66 Structural Characterisation of Btrk Decarboxylase from Bacillus Circulans Butirosin Biosynthesis
• Chain: A
• Resolution: 1.65 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K49 Y187 E269
• Catalytic site (residue number reindexed from 1): K46 Y182 E262
• Enzyme Commision number: 4.1.1.95: L-glutamyl-[BtrI acyl-carrier protein] decarboxylase.

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	PLP	A	S47 K49 E68 Y187 T190 E269 S270 G271 R272 Y375	S44 K46 E65 Y182 T185 E262 S263 G264 R265 Y348

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0008836 diaminopimelate decarboxylase activity
• GO:0016830 carbon-carbon lyase activity
• GO:0016831 carboxy-lyase activity
• GO:0042803 protein homodimerization activity

Biological Process

• GO:0009089 lysine biosynthetic process via diaminopimelate
• GO:0017000 antibiotic biosynthetic process

External links

• PDB: RCSB:2j66, PDBe:2j66, PDBj:2j66
• PDBsum: 2j66
• UniProt: Q2L4H3|BTRK_NIACI L-glutamyl-[BtrI acyl-carrier protein] decarboxylase (Gene Name=btrK)