Structure of PDB 2c81 Chain A

Receptor sequence
>2c81A (length=408) Species: 1397 (Niallia circulans) [Search protein sequence]
WPEWPQHSDRTRRKIEEVFQSNRWAISGYWTGEESMERKFAKAFADFNGV
PYCVPTTSGSTALMLALEALGIGEGDEVIVPSLTWIATATAVLNVNALPV
FVDVEADTYCIDPQLIKSAITDKTKAIIPVHLFGSMANMDEINEIAQEHN
LFVIEDCAQSHGSVWNNQRAGTIGDIGAFSCQQGKVLTAGEGGIIVTKNP
RLFELIQQLRADSRVYCDDSSELMHGDMQLVKKGDIQGSNYCLSEFQSAI
LLDQLQELDDKNAIREKNAMFLNDALSKIDGIKVMKRPPQVSRQTYYGYV
FRFDPVKFGGLNADQFCEILREKLNMGTFYLHPPYLPVHKNPLFCPWTKN
RYLKSVRKTEAYWRGLHYPVSERASGQSIVIHHAILLAEPSHLSLLVDAV
AELARKFC
3D structure
PDB2c81 Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W92 D163 Q166 Q189 K192 D225 K239 C249
Catalytic site (residue number reindexed from 1) W85 D156 Q159 Q182 K185 D218 K232 C242
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 PMP A S65 G66 S67 W92 D163 A165 Q166 S187 K192 C415 S58 G59 S60 W85 D156 A158 Q159 S180 K185 C408
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

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Molecular Function
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Biological Process
External links
PDB RCSB:2c81, PDBe:2c81, PDBj:2c81
PDBsum2c81
PubMed16894611
UniProtQ8G8Y2|GLDSA_NIACI L-glutamine:2-deoxy-scyllo-inosose aminotransferase (Gene Name=btrR)

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