Structure of PDB 4q0w Chain A

Receptor sequence
>4q0wA (length=316) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
GVHSFWDIAGPTARPVRLESLEDKRMAVDASIWIYQFLKAVRDQNAVKNS
HITGFFRRICKLLYFGIRPVFVFDGGVPVLKRETIRQRKERRQGKREDEV
TMDMIKEVQELLSRFGIPYITAPMEAEAQCAELLQLNLVDGIITDDSDVF
LFGGTKIYKNMFHEKNYVEFYDAESILKLLGLDRKNMIELAQLLGSDYTN
GLKGMGPVSSIEVIAEFGNLKNFKDWYNNGQFDKRKQETENKFEKDLRKK
LVNNEIILDDDFPSVMVYDAYMRPEVDHDTTPFVWGVPDLDMLRSFMKTQ
LGWPHEKSDEILIPLI
3D structure
PDB4q0w Crystal structure of the catalytic core of Rad2: insights into the mechanism of substrate binding.
ChainA
Resolution2.1 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.1.-.-
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 W7 Y36 Q37 K40 D812 D813 S814 K826 W6 Y35 Q36 K39 D145 D146 S147 K159
BS02 dna A Q37 A41 R95 G871 G873 P874 V875 S876 Q36 A40 R92 G204 G206 P207 V208 S209
BS03 CA A E794 D813 D815 E127 D146 D148
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003697 single-stranded DNA binding
GO:0003824 catalytic activity
GO:0004518 nuclease activity
GO:0004519 endonuclease activity
GO:0016788 hydrolase activity, acting on ester bonds
Biological Process
GO:0006289 nucleotide-excision repair
Cellular Component
GO:0005634 nucleus

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4q0w, PDBe:4q0w, PDBj:4q0w
PDBsum4q0w
PubMed25120270
UniProtP07276|RAD2_YEAST DNA repair protein RAD2 (Gene Name=RAD2)

[Back to BioLiP]