Structure of PDB 3u4q Chain A

Receptor sequence
>3u4qA (length=1122) Species: 1423 (Bacillus subtilis) [Search protein sequence]
TWTDDQWNAIVSTGQDILVAAAAGSGKTAVLVERMIRKITAEENPIDVDR
LLVVTFTNASAAEMKHRIAEALEKELVQRPGSLHIRRQLSLLNRASISTL
HSFCLQVLKKYYYLIDLDPGFRIADQTEGELIGDEVLDELFEDEYAKGEK
AFFELVDRYTTDRHDLDLQFLVKQVYEYSRSHPNPEAWLESFVHLYDVSE
KSAIEELPFYQYVKEDIAMVLNGAKEKLLRALELTDNFLDDLAQIDELIQ
HQDDFSELYKRVPAVSDPALLDEATDLRNGAKKLLEKLKTDYFTRSPEQH
LKSLAEMKPVIETLVQLVISYGKRFEAAKQEKSIIDFSDLEHYCLAILTA
ENDREPSEAARFYQEQFHEVLVDEYQDTNLVQESILQLVTSGPEETGNLF
MVGDVKQSIYRFRLAEPLLFLSKYKRFTESGEGTGRKIDLNKNFRSRADI
LDSTNFLFKQLMGGKIGEVDYDEQAELKLGAAYPDNDETETELLLIDLET
VQFEAKAIAKEIRKLISSPFKVYKKTHRNIQYRDIVILLRSMPWAPQIME
ELRAQGIPVYANLTSGYFEAVEVAVALSVLKVIDNPYQDIPLASVLRSPI
VGADENELSLIRLENKKAPYYEAMKDYLAAGDRSDELYQKLNTFYGHLQK
WRAFSKNHSVSELIWEVYRDTKYMDYVGGMPGGKQRQANLRVLYDRARQY
ESTAFRGLFRFLRFIERMQERGDQEDVVRLMTIHSSKGLEFPVVFVAGLG
RNFNMMDLNKSYLLDKELGFGTKYIHPQLRISYPTLPLIAMKKKMRRELL
SEELRVLYVALTRAKEKLFLIGSCKDHQKQLAKWQASASQTDWLLPEFDR
YQARTYLDFIGPALARHRHADISGHPARFAVQMIHSYDSERLEAIRRGEP
VFAFDEKAREQLSWTYPHQEVTQIRTKQSVSDEYSGRYRRPAFMMKKGLT
AAEKGTAMHTVMQHIPLSHVPSIEEAEQTVHRLYEKELLTEEQKDAIDIE
EIVQFFHTEIGGQLIGAKWKDREIPFSLALPAKEIYPDAHEADEPLLVQG
IIDCLYETEDGLYLLAYKSDRIEGGFEGAAPILKKRYETQIQLYTKAVEQ
IAKTKVKGCALYFFDGGHILTL
3D structure
PDB3u4q Insights into Chi recognition from the structure of an AddAB-type helicase-nuclease complex.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K36 T37 D407 E408 Q441 R873
Catalytic site (residue number reindexed from 1) K27 T28 D373 E374 Q407 R813
Enzyme Commision number 3.1.-.-
5.6.2.4: DNA 3'-5' helicase.
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 dna A F65 E408 D411 Y444 F446 R590 S591 T792 H794 R811 N812 N814 D817 F56 E374 D377 Y410 F412 R540 S541 T732 H734 R751 N752 N754 D757
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003678 DNA helicase activity
GO:0003690 double-stranded DNA binding
GO:0004386 helicase activity
GO:0004527 exonuclease activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008408 3'-5' exonuclease activity
GO:0016787 hydrolase activity
GO:0016853 isomerase activity
GO:0016887 ATP hydrolysis activity
GO:0043138 3'-5' DNA helicase activity
Biological Process
GO:0000724 double-strand break repair via homologous recombination
GO:0000725 recombinational repair
GO:0006281 DNA repair
GO:0006302 double-strand break repair
GO:0032508 DNA duplex unwinding
Cellular Component
GO:0005829 cytosol
GO:0033202 DNA helicase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3u4q, PDBe:3u4q, PDBj:3u4q
PDBsum3u4q
PubMed22307084
UniProtP23478|ADDA_BACSU ATP-dependent helicase/nuclease subunit A (Gene Name=addA)

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