Structure of PDB 2xrz Chain B Binding Site BS01

Receptor Information
>2xrz Chain B (length=434) Species: 192952 (Methanosarcina mazei Go1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LVPRGSHMNPKRIRALKSGKQGDGPVVYWMSRDQRAEDNWALLFSRAIAK
EANVPVVVVFCLTDEFLEAGIRQYEFMLKGLQELEVSLSRKKIPSFFLRG
DPGEKISRFVKDYNAGTLVTDFSPLRIKNQWIEKVISGISIPFFEVDAHN
VVPCWEASQKHEYAAHTFRPKLYALLPEFLEEFPELEPNSVTKDPLFEPW
HFEPGEKAAKKVMESFIADRLDSYGALRNDPTKNMLSNLSPYLHFGQISS
QRVVLEVEKAESNPGSKKAFLDEILIWKEISDNFCYYNPGYDGFESFPSW
AKESLNAHRNDVRSHIYTLEEFEAGKTHDPLWNASQMELLSTGKMHGYTR
MYWAKKILEWSESPEKALEIAICLNDRYELDGRDPNGYAGIAWSIGGVHD
RAWGEREVTGKIRYMSYEGCKRKFDVKLYIEKYS
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2xrz Crystal Structures of an Archaeal Class II DNA Photolyase and its Complex with Uv-Damaged Duplex DNA.
Resolution2.2 Å
Binding residue
(original residue number in PDB)
A160 H161 N257 E301 W305 M379 W421 R429 W431 R441 Y442 M443 S444 R450 K451
Binding residue
(residue number reindexed from 1)
A165 H166 N229 E273 W277 M351 W393 R401 W403 R413 Y414 M415 S416 R422 K423
Binding affinityPDBbind-CN: Kd=44nM
Enzymatic activity
Catalytic site (original residue number in PDB) E301 W305 A335 G375
Catalytic site (residue number reindexed from 1) E273 W277 A307 G347
Enzyme Commision number 4.1.99.3: deoxyribodipyrimidine photo-lyase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003677 DNA binding
GO:0003904 deoxyribodipyrimidine photo-lyase activity
GO:0016829 lyase activity
Biological Process
GO:0000719 photoreactive repair
GO:0006281 DNA repair

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:2xrz, PDBe:2xrz, PDBj:2xrz
PDBsum2xrz
PubMed21892138
UniProtQ8PYK9

[Back to BioLiP]