Structure of PDB 2c7t Chain A

Receptor sequence

>2c7tA (length=411) Species: 1397 (Niallia circulans)

DHWPEWPQHSDRTRRKIEEVFQSNRWAISGYWTGEESMERKFAKAFADFN
GVPYCVPTTSGSTALMLALEALGIGEGDEVIVPSLTWIATATAVLNVNAL
PVFVDVEADTYCIDPQLIKSAITDKTKAIIPVHLFGSMANMDEINEIAQE
HNLFVIEDCAQSHGSVWNNQRAGTIGDIGAFSCQQGKVLTAGEGGIIVTK
NPRLFELIQQLRADSRVYCDDSSELMHGDMQLVKKGDIQGSNYCLSEFQS
AILLDQLQELDDKNAIREKNAMFLNDALSKIDGIKVMKRPPQVSRQTYYG
YVFRFDPVKFGGLNADQFCEILREKLNMGTFYLHPPYLPVHKNPLFCPWT
KNRYLKSVRKTEAYWRGLHYPVSERASGQSIVIHHAILLAEPSHLSLLVD
AVAELARKFCV

3D structure

• PDB: 2c7t Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis.
• Chain: A
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): W92 D163 Q166 Q189 K192 D225 K239 C249
• Catalytic site (residue number reindexed from 1): W87 D158 Q161 Q184 K187 D220 K234 C244
• Enzyme Commision number: 2.6.1.100: L-glutamine:2-deoxy-scyllo-inosose aminotransferase.
  2.6.1.101: L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase.

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	G66 S67 W92 D163 A165 Q166 S187 K192 C415 V416	G61 S62 W87 D158 A160 Q161 S182 K187 C410 V411

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0008483 transaminase activity
• GO:0030170 pyridoxal phosphate binding

Biological Process

• GO:0000271 polysaccharide biosynthetic process
• GO:0017000 antibiotic biosynthetic process

External links

• PDB: RCSB:2c7t, PDBe:2c7t, PDBj:2c7t
• PDBsum: 2c7t
• PubMed: 16894611
• UniProt: Q8G8Y2|GLDSA_NIACI L-glutamine:2-deoxy-scyllo-inosose aminotransferase (Gene Name=btrR)