Structure of PDB 4q0z Chain B

Receptor sequence
>4q0zB (length=307) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
GVHSFWDIAGPTARPVRLESLEDKRMAVDASIWIYQFLKAVRDQNAVKNS
HITGFFRRICKLLYFGIRPVFVFDGGVPVLKRETIRQSDEVTMDMIKEVQ
ELLSRFGIPYITAPMEAEAQCAELLQLNLVDGIITDDSDVFLFGGTKIYK
NMFHEKNYVEFYDAESILKLLGLDRKNMIELAQLLGSDYTNGLKGMGPVS
SIEVIAEFGNLKNFKDWYNNGQFDKRKQETENKFEKDLRKKLVNNEIILD
DDFPSVMVYDAYMRPEVDHDTTPFVWGVPDLDMLRSFMKTQLGWPHEKSD
EILIPLI
3D structure
PDB4q0z Crystal structure of the catalytic core of Rad2: insights into the mechanism of substrate binding.
ChainB
Resolution2.398 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 B Y36 Q37 K40 E766 V767 K909 K916 Y35 Q36 K39 E90 V91 K233 K240
BS02 dna B A41 G871 G873 P874 V875 S876 A40 G195 G197 P198 V199 S200
BS03 CA B E794 D813 D815 E118 D137 D139
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:4q0z, PDBe:4q0z, PDBj:4q0z
PDBsum4q0z
PubMed25120270
UniProtP07276|RAD2_YEAST DNA repair protein RAD2 (Gene Name=RAD2)

[Back to BioLiP]