Structure of PDB 6ojt Chain A

Receptor sequence
>6ojtA (length=481) Species: 13689 (Sphingomonas paucimobilis) [Search protein sequence]
AHFPQTPGFSGTLRPLRIEGDILDIEIEGEVPPQLNGTFHRVHPDAQFPP
RFEDDQFFNGDGMVSLFRFHDGKIDFRQRYAQTDKWKVERKAGKSLFGAY
RNPLTDDASVQGMIRGTANTNVMVHAGKLYAMKEDSPCLIMDPLTLETEG
YTNFDGKLQSQTFCAHPKIDPVTGNLCAFAYGAKGLMTLDMAYIEISPTG
KLLKEIPFQNPYYCMMHDFGVTEDYAVFAVMPLLSSWDRLEQRLPFFGFD
TTLPCYLGILPRNGDARDLRWFKTGNCFVGHVMNAFNDGTKVHIDMPVSR
NNSFPFFDVHGAPFDPVAGQGFLTRWTVDMASNGDSFEKTERLFDRPDEF
PRIDERYATRAYRHGWMLILDTEKPYEAPGGAFYALTNTLGHIDLATGKS
SSWWAGPRCAIQEPCFIPRSPDAPEGDGYVIALVDDHVANYSDLAIFDAQ
HVDQGPIARAKLPVRIRQGLHGNWADASRLA
3D structure
PDB6ojt Identification of functionally important residues and structural features in a bacterial lignostilbene dioxygenase.
ChainA
Resolution3.0 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 1.13.11.43: lignostilbene alphabeta-dioxygenase.
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 NSL A F59 Y101 K134 E135 H218 H282 F308 F58 Y100 K133 E134 H217 H281 F307
BS02 FE A H167 H218 H282 H472 H166 H217 H281 H471
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0010436 carotenoid dioxygenase activity
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0046872 metal ion binding
GO:0050054 lignostilbene alpha beta-dioxygenase activity
GO:0051213 dioxygenase activity
Biological Process
GO:0016121 carotene catabolic process
GO:0046274 lignin catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6ojt, PDBe:6ojt, PDBj:6ojt
PDBsum6ojt
PubMed31292192
UniProtQ53353|LSDX1_SPHPI Lignostilbene-alpha,beta-dioxygenase isozyme I

[Back to BioLiP]