Structure of PDB 6d3m Chain A Binding Site BS01
Receptor Information
>6d3m Chain A (length=286) Species:
76947
(Sphingobium herbicidovorans) [
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NKYRFIDVQPLTGVLGAEITGVDLREPLDDSTWNEILDAFHTYQVIYFPG
QAITNEQHIAFSRRFGPVDPVPILKSIEGYPEVQMIRREANESSRFIGDD
WHTDSTFLDAPPAAVVMRAIEVPEYGGDTGFLSMYSAWETLSPTMQATIE
GLNVVHSATKVFGSLYQATNWRFSNTSVKVMDVDAGDRETVHPLVVTHPV
TGRRALYCNQVYCQKIQGMTDAESKSLLQFLYEHATKFDFTCRVRWKKDQ
VLVWDNLCTMHRAVPDYAGKFRYLTRTTVAGDKPSR
Ligand information
Ligand ID
CO
InChI
InChI=1S/Co/q+2
InChIKey
XLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Co+2]
CACTVS 3.341
[Co++]
Formula
Co
Name
COBALT (II) ION
ChEMBL
DrugBank
DB14205
ZINC
PDB chain
6d3m Chain A Residue 301 [
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Receptor-Ligand Complex Structure
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PDB
6d3m
Development of enzymes for robust aryloxyphenoxypropionate and synthetic auxin herbicide tolerance traits in maize and soybean crops.
Resolution
2.03 Å
Binding residue
(original residue number in PDB)
H111 D113 H270
Binding residue
(residue number reindexed from 1)
H102 D104 H261
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H111 D113 H270 R285
Catalytic site (residue number reindexed from 1)
H102 D104 H261 R276
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:6d3m
,
PDBe:6d3m
,
PDBj:6d3m
PDBsum
6d3m
PubMed
30828945
UniProt
Q8KSC8
|RDPA_SPHHM (R)-phenoxypropionate/alpha-ketoglutarate-dioxygenase (Gene Name=rdpA)
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