Structure of PDB 6d0o Chain A Binding Site BS02
Receptor Information
>6d0o Chain A (length=274) Species:
1219045
(Sphingobium herbicidovorans NBRC 16415) [
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QRFERIAVQPLTGVLGAEITGVDLREPLDDSTWNEILDAFHTYQVIYFPG
QAITNEQHIAFSRRFGPVDPVPLLKSIEGYPEVQMIRRIGDDWHTDSTFL
DAPPAAVVMRAIDVPEHGGDTGFLSMYTAWETLSPTMQATIEGLNVVHSA
TRVFGSLYQAQNRMDVDAGDRETVHPLVVTHPGSGRKGLYVNQVYCQRIE
GMSEKESEPLLSFLFAHATKPEFTCRVRWKKDQVVVWDNLCTMHYAINDY
HGQTRILHRTTVGGVRPARHHHHH
Ligand information
Ligand ID
AKG
InChI
InChI=1S/C5H6O5/c6-3(5(9)10)1-2-4(7)8/h1-2H2,(H,7,8)(H,9,10)
InChIKey
KPGXRSRHYNQIFN-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
O=C(O)C(=O)CCC(=O)O
OpenEye OEToolkits 1.7.6
C(CC(=O)O)C(=O)C(=O)O
CACTVS 3.385
OC(=O)CCC(=O)C(O)=O
Formula
C5 H6 O5
Name
2-OXOGLUTARIC ACID
ChEMBL
CHEMBL1686
DrugBank
DB08845
ZINC
ZINC000001532519
PDB chain
6d0o Chain A Residue 402 [
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Receptor-Ligand Complex Structure
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PDB
6d0o
Development of enzymes for robust aryloxyphenoxypropionate and synthetic auxin herbicide tolerance traits in maize and soybean crops.
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
H111 D113 H270 R281
Binding residue
(residue number reindexed from 1)
H94 D96 H244 R255
Annotation score
5
Enzymatic activity
Catalytic site (original residue number in PDB)
H111 D113 H270 R285
Catalytic site (residue number reindexed from 1)
H94 D96 H244 R259
Enzyme Commision number
1.14.11.44
: (R)-dichlorprop dioxygenase (2-oxoglutarate).
Gene Ontology
Molecular Function
GO:0016491
oxidoreductase activity
GO:0016706
2-oxoglutarate-dependent dioxygenase activity
GO:0046872
metal ion binding
GO:0051213
dioxygenase activity
Biological Process
GO:0009056
catabolic process
Cellular Component
GO:0005737
cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:6d0o
,
PDBe:6d0o
,
PDBj:6d0o
PDBsum
6d0o
PubMed
30828945
UniProt
Q8KSC8
|RDPA_SPHHM (R)-phenoxypropionate/alpha-ketoglutarate-dioxygenase (Gene Name=rdpA)
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