Structure of PDB 7pmm Chain B Binding Site BS01
Receptor Information
>7pmm Chain B (length=439) Species:
83333
(Escherichia coli K-12) [
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GMTAFSTLNVLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKT
GSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQVAGELRRLARFLP
NTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNT
LVMDEADRMLDMGFSDAIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQ
RDPLAIEIDSTDALPPIEQQFYETSSKGKIPLLQRLLSLHQPSSCVVFCN
TKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATD
VAARGLDIKSLELVVNFELAWDPEVHVHRIGRTARAGNSGLAISFCAPEE
AQRANIISDMLQIKLNWQTPPANSSIATLEAEMATLCIDGGKKAKMRPGD
VLGADIGKIAVHPAHVYVAVRQAWKQLQIKGKTCRVRLL
Ligand information
>7pmm Chain C (length=42) [
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gggaacccuucccaaauggcuguucgccauuugggaaggguu
...<<<<<<<<<<<<<<<<<.....>>>>>>>>>>>>>>>>>
Receptor-Ligand Complex Structure
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PDB
7pmm
Structural basis for RNA-duplex unwinding by the DEAD-box helicase DbpA.
Resolution
3.0 Å
Binding residue
(original residue number in PDB)
N100 T101 K102 S118 H121 K391 K394 R396 P397 G398 D399 L401 I415 G416 K417 I418 K447
Binding residue
(residue number reindexed from 1)
N101 T102 K103 S119 H122 K392 K395 R397 P398 G399 D400 L402 I406 G407 K408 I409 K430
Enzymatic activity
Enzyme Commision number
3.6.4.13
: RNA helicase.
Gene Ontology
Molecular Function
GO:0003676
nucleic acid binding
GO:0003723
RNA binding
GO:0003724
RNA helicase activity
GO:0004386
helicase activity
GO:0005524
ATP binding
GO:0016787
hydrolase activity
GO:0016887
ATP hydrolysis activity
GO:0019843
rRNA binding
GO:0033677
DNA/RNA helicase activity
GO:0034458
3'-5' RNA helicase activity
GO:0043531
ADP binding
Biological Process
GO:0000027
ribosomal large subunit assembly
GO:0042254
ribosome biogenesis
Cellular Component
GO:0005737
cytoplasm
GO:0005829
cytosol
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:7pmm
,
PDBe:7pmm
,
PDBj:7pmm
PDBsum
7pmm
PubMed
37221012
UniProt
P21693
|DBPA_ECOLI ATP-dependent RNA helicase DbpA (Gene Name=dbpA)
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