Structure of PDB 2y1j Chain A Binding Site BS02

Receptor Information
>2y1j 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
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PDB2y1j Crystal Structures and Repair Studies Reveal the Identity and the Base-Pairing Properties of the Uv-Induced Spore Photoproduct DNA Lesion.
Resolution2.15 Å
Binding residue
(original residue number in PDB)
N529 S530 L610 T611 Q612 T613 S617 S618 T619 N622 N625 Y714 R771 F786 M790 N793 Q797
Binding residue
(residue number reindexed from 1)
N233 S234 L314 T315 Q316 T317 S321 S322 T323 N326 N329 Y418 R475 F490 M494 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:2y1j, PDBe:2y1j, PDBj:2y1j
PDBsum2y1j
PubMed21780197
UniProtE1C9K5

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