Structure of PDB 6d3j Chain A Binding Site BS03

Receptor Information
>6d3j Chain A (length=247) Species: 76947 (Sphingobium herbicidovorans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NKYRFIDVQPLTGVLGAEITGVDLREPLDDSTWNEILDAFHTYQVIYFPG
QAITNEQHIAFSRRFGPVDPVPILKSIEGYPEVQMIRIGDDWHTDSTFLD
APPAAVVMRAIEVPEYGGDTGFLSMYSAWETLSPTMQATIEGLNVVHSAE
TVHPLVVTHPVTGRRALYCNQVYCQKIQGMTDAESKSLLQFLYEHATKFD
FTCRVRWKKDQVLVWDNLCTMHRAVPDYAGKFRYLTRTTVAGDKPSR
Ligand information
Ligand IDCO
InChIInChI=1S/Co/q+2
InChIKeyXLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Co+2]
CACTVS 3.341[Co++]
FormulaCo
NameCOBALT (II) ION
ChEMBL
DrugBankDB14205
ZINC
PDB chain6d3j Chain A Residue 306 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6d3j Development of enzymes for robust aryloxyphenoxypropionate and synthetic auxin herbicide tolerance traits in maize and soybean crops.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		P76 V77
Binding residue
(residue number reindexed from 1)		P67 V68
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H111 D113 H270 R285
Catalytic site (residue number reindexed from 1) H93 D95 H222 R237
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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Biological Process
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Cellular Component
External links
PDB RCSB:6d3j, PDBe:6d3j, PDBj:6d3j
PDBsum6d3j
PubMed30828945
UniProtQ8KSC8|RDPA_SPHHM (R)-phenoxypropionate/alpha-ketoglutarate-dioxygenase (Gene Name=rdpA)

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