Structure of PDB 5fm7 Chain B

Receptor sequence
>5fm7B (length=422) Species: 209285 (Thermochaetoides thermophila) [Search protein sequence]
SVTETKELIAAHSHIRGLGVDADTLEPRPSSQGLVGQEKARKAAAVVLEM
IKQGKIAGRAVLIAGPPSTGKTAIAMGMAQSLGQDVPFTTLAASEIFSLE
MSKTEALTQAFRKSIGVRIKEESEIMEGEVVEIQIDRKLTIKTTDMEAIY
DMGSKMIDAMTKERVMAGDIISIDKSSGKITKLGRSYAKFLQCPEGELQK
RKEVVHTVSLHEIDVINSRTQGFLALFSGDTGEIRSEIRDQINTKVAEWK
EEGKAEIVPGVLFIDEVHMLDIECFSYINRALESDLAPIVIMASNRGVSR
IRGTDYKSPHGLPLDFLDRVVIINTHPYTPDELRQILSIRAQEEEVDLTP
DALALLTKIGQEAGLRYASNLITTSQLIAAKRRAKQVGVEDVQRSFKLFY
DPARSVRFVQESEKRLIGNDGV
3D structure
PDB5fm7 The Combination of X-Ray Crystallography and Cryo-Electron Microscopy Provides Insight Into the Overall Architecture of the Dodecameric Rvb1/Rvb2 Complex.
ChainB
Resolution2.901 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.4.12: DNA 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 ADP B H24 H26 L46 V47 T81 G82 K83 T84 Y361 I369 L398 H12 H14 L34 V35 T69 G70 K71 T72 Y328 I336 L365
Gene Ontology
Molecular Function
GO:0003678 DNA helicase activity
GO:0004386 helicase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008094 ATP-dependent activity, acting on DNA
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0000492 box C/D snoRNP assembly
GO:0006281 DNA repair
GO:0006325 chromatin organization
GO:0006338 chromatin remodeling
GO:0006357 regulation of transcription by RNA polymerase II
GO:0032508 DNA duplex unwinding
Cellular Component
GO:0000812 Swr1 complex
GO:0005634 nucleus
GO:0031011 Ino80 complex
GO:0035267 NuA4 histone acetyltransferase complex
GO:0097255 R2TP complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5fm7, PDBe:5fm7, PDBj:5fm7
PDBsum5fm7
PubMed26745716
UniProtG0RYC2

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