Structure of PDB 7q05 Chain E

Receptor sequence
>7q05E (length=409) Species: 34028 (Comamonas sp.) [Search protein sequence]
ESIIQWHGATNTRVPFGIYTDTANADQEQQRIYRGEVWNYLCLESEIPGA
GDFRTTFAGETPIVVVRDADQEIYAFENRCAHRGALIALEKSGRTDSFQC
VYHAWSYNRQGDLTGVAFEKGVKGQGGMPASFCKEEHGPRKLRVAVFCGL
VFGSFSEDVPSIEDYLGPEICERIERVLHKPVEVIGRFTQKLPNNWKLYF
ENVKDSYHASLLHMFFTTFELNRLSQKGGVIVDESGGHHVSYSMIDRGAK
DRLKDPSLLEGFEEFEDGVTLQILSVFPGFVLQQIQNSIAVRQLLPKSIS
SSELNWTYLGYADDSAEQRKVRLKQANLIGPAGFISMEDGAVGGFVQRGI
AGAANLDAVIEMGGDHEGSSEGRATETSVRGFWKAYRKHMGQEMQAENLY
FQGHHHHHH
3D structure
PDB7q05 Biochemical and structural characterization of an aromatic ring-hydroxylating dioxygenase for terephthalic acid catabolism.
ChainE
Resolution2.08 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.12.15: terephthalate 1,2-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 FES E C82 H84 R85 C102 Y104 H105 W107 C80 H82 R83 C100 Y102 H103 W105
BS02 UB7 E V205 A211 S243 L288 I290 R309 D356 V203 A209 S241 L271 I273 R292 D339
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0018628 terephthalate 1,2-dioxygenase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:0018963 phthalate metabolic process
GO:0044237 cellular metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:7q05, PDBe:7q05, PDBj:7q05
PDBsum7q05
PubMed35312352
UniProtQ3C1D5|TPDA2_COMSP Terephthalate 1,2-dioxygenase, terminal oxygenase component subunit alpha 2 (Gene Name=tphA2II)

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