Structure of PDB 5w71 Chain A Binding Site BS01
Receptor Information
>5w71 Chain A (length=413) Species:
1397
(Niallia circulans) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
IPFDHWPEWPQHSDRTRRKIEEVFQSNRWAISGYWTGEESMERKFAKAFA
DFNGVPYCVPTTSGSTALMLALEALGIGEGDEVIVPSLTWIATATAVLNV
NALPVFVDVEADTYCIDPQLIKSAITDKTKAIIPVHLFGSMANMDEINEI
AQEHNLFVIEDCAQSHGSVWNNQRAGTIGDIGAFSCQQGKVLTAGEGGII
VTKNPRLFELIQQLRADSRVYCDDSSELMHGDMQLVKKGDIQGSNYCLSE
FQSAILLDQLQELDDKNAIREKNAMFLNDALSKIDGIKVMKRPPQVSRQT
YYGYVFRFDPVKFGGLNADQFCEILREKLNMGTFYLHPPYLPVHKNPLFC
PWTKNRYLKSVRKTEAYWRGLHYPVSERASGQSIVIHHAILLAEPSHLSL
LVDAVAELARKFC
Ligand information
Ligand ID
PLP
InChI
InChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
InChIKey
NGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0
Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04
O=P(O)(O)OCc1cnc(c(O)c1C=O)C
Formula
C8 H10 N O6 P
Name
PYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBL
CHEMBL82202
DrugBank
DB00114
ZINC
ZINC000001532514
PDB chain
5w71 Chain A Residue 501 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
5w71
The structure of RbmB from Streptomyces ribosidificus, an aminotransferase involved in the biosynthesis of ribostamycin.
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
S65 G66 S67 W92 D163 A165 Q166 S187 K192
Binding residue
(residue number reindexed from 1)
S63 G64 S65 W90 D161 A163 Q164 S185 K190
Annotation score
1
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.
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
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:5w71
,
PDBe:5w71
,
PDBj:5w71
PDBsum
5w71
PubMed
28685903
UniProt
Q8G8Y2
|GLDSA_NIACI L-glutamine:2-deoxy-scyllo-inosose aminotransferase (Gene Name=btrR)
[
Back to BioLiP
]