Structure of PDB 2y1i Chain A Binding Site BS02

Receptor Information
>2y1i Chain A (length=580) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AKMAFTLADRVTEEMLADKAALVVEVVEENYHDAPIVGIAVVNEHGRFFL
RPESALADPQFVAWLGDETKKKSMFDSKRAAVALKWKGIELCGVSFDLLL
AAYLLDPAQGVDDVAAAAKMKQYEAVRPDEAVYGKGAKRAVPDEPVLAEH
LVRKAAAIWALERPFLDELRRNEQDRLLVELEQPLSSILAEMEFAGVKVD
TKRLEQMGKELAEQLRTVEQRIYELAGQEFNINSPKQLGVILFEKLQLPV
LKKTKTGYSTSADVLEKLAPYHEIVENILHYRQLGKLQSTYIEGLLKVVR
PDTKKVHTIFNQALTQTGRLSSTEPNLQNIPIRLEEGRKIRQAFVPSESD
WLIFAADYSQIELRVLAHIAEDDNLMEAFRRDLDIHTKTAMDIFQVSEDE
VTPNMRRQAKAVNKGIVYGISDYGLAQNLNISRKEAAEFIERYFESFPGV
KRYMENIVQEAKQKGYVTTLLHRRRYLPDITSRNFNVRSFAERMAMNTPI
QGSAADIIKKAMIDLNARLKEERLQARLLLQVHDELILEAPKEEMERLCR
LVPEVMEQAVTLRVPLKVDYHYGSTWYDAK
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2y1i Crystal Structures and Repair Studies Reveal the Identity and the Base-Pairing Properties of the Uv-Induced Spore Photoproduct DNA Lesion.
Resolution2.78 Å
Binding residue
(original residue number in PDB)		N529 S530 L610 T611 Q612 S617 T619 N622 Y714 R771 F786 N793 Q797
Binding residue
(residue number reindexed from 1)		N233 S234 L314 T315 Q316 S321 T323 N326 Y418 R475 F490 N497 Q501
Enzymatic activity
Enzyme Commision number 2.7.7.7: DNA-directed DNA polymerase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0003677 DNA binding
GO:0003887 DNA-directed DNA polymerase activity
GO:0004518 nuclease activity
GO:0008408 3'-5' exonuclease activity
GO:0046872 metal ion binding
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006260 DNA replication
GO:0006261 DNA-templated DNA replication
GO:0006281 DNA repair
GO:0006302 double-strand break repair
GO:0006974 DNA damage response
GO:0071897 DNA biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2y1i, PDBe:2y1i, PDBj:2y1i
PDBsum2y1i
PubMed21780197
UniProtE1C9K5

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