Structure of PDB 5w71 Chain A

Receptor sequence
>5w71A (length=413) Species: 1397 (Niallia circulans) [Search protein sequence]
IPFDHWPEWPQHSDRTRRKIEEVFQSNRWAISGYWTGEESMERKFAKAFA
DFNGVPYCVPTTSGSTALMLALEALGIGEGDEVIVPSLTWIATATAVLNV
NALPVFVDVEADTYCIDPQLIKSAITDKTKAIIPVHLFGSMANMDEINEI
AQEHNLFVIEDCAQSHGSVWNNQRAGTIGDIGAFSCQQGKVLTAGEGGII
VTKNPRLFELIQQLRADSRVYCDDSSELMHGDMQLVKKGDIQGSNYCLSE
FQSAILLDQLQELDDKNAIREKNAMFLNDALSKIDGIKVMKRPPQVSRQT
YYGYVFRFDPVKFGGLNADQFCEILREKLNMGTFYLHPPYLPVHKNPLFC
PWTKNRYLKSVRKTEAYWRGLHYPVSERASGQSIVIHHAILLAEPSHLSL
LVDAVAELARKFC
3D structure
PDB5w71 The structure of RbmB from Streptomyces ribosidificus, an aminotransferase involved in the biosynthesis of ribostamycin.
ChainA
Resolution2.1 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) W90 D161 Q164 Q187 K190 D223 K237 C247
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 S65 G66 S67 W92 D163 A165 Q166 S187 K192 S63 G64 S65 W90 D161 A163 Q164 S185 K190
BS02 9YM A R221 N247 R219 N245
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:5w71, PDBe:5w71, PDBj:5w71
PDBsum5w71
PubMed28685903
UniProtQ8G8Y2|GLDSA_NIACI L-glutamine:2-deoxy-scyllo-inosose aminotransferase (Gene Name=btrR)

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