Structure of PDB 2fdc Chain A

Receptor sequence
>2fdcA (length=505) Species: 1395 ([Bacillus] caldotenax) [Search protein sequence]
VEGRFQLVAPYEPQGDQPQAIAKLVDGLRRGVKHQTLLGATGTGKTFTIS
NVIAQVNKPTLVIAHNKTLAGQLYSELKEFFPHNAVEYFVSYYDYYQPEA
YVPQTDTYIEKDAKINDEIDKLRHSATSALFERRDVIIVASVSCIYGLGS
PEEYRELVVIFPASHFVTREEKMRLAIQNIEQELEERLAELRAQGKLLEA
QRLEQRTRYDLEMMREMGFCSGIENYSRHLALRPPGSTPYTLLDYFPDDF
LIIVDESHVTLPQLRGMYNGDRARKQVLVDHGFRLPSALDNRPLTFEEFE
QKINQIIYVSATPGPYELEHSPGVVEQIIRPTGLLDPTIDVRPTKGQIDD
LIGEIRERVERNERTLVTTLTKKMAEDLTDYLKEAGIKVAYLHERIEIIR
DLRLGKYDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIG
RAARNANGHVIMYADTITKSMEIAIQETKRRRAIQEEYNRKHGIVPRTVK
KEIRD
3D structure
PDB2fdc Structural basis for DNA recognition and processing by UvrB.
ChainA
Resolution3.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 H65 S91 Y92 Y93 Y96 P98 K111 S141 S143 Y146 F249 F302 S304 I306 E307 S310 Q346 M350 R357 H65 S91 Y92 Y93 Y96 P98 K111 S141 S143 Y146 F166 F219 S221 I223 E224 S227 Q263 M267 R274
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0006289 nucleotide-excision repair
Cellular Component
GO:0009380 excinuclease repair complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2fdc, PDBe:2fdc, PDBj:2fdc
PDBsum2fdc
PubMed16532007
UniProtP56981|UVRB_BACCA UvrABC system protein B (Gene Name=uvrB)

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