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PDBsum entry 7uvc
Go to PDB code:
Transferase/ligase
PDB id
7uvc
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Contents
Protein chains
149 a.a.
160 a.a.
PDB id:
7uvc
Links
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Sacch3D
Name:
Transferase/ligase
Title:
Rad6(p43l)-bre1 complex
Structure:
Ubiquitin-conjugating enzyme e2 2. Chain: a. Synonym: e2 ubiquitin-conjugating enzyme 2,radiation sensitivity protein 6,ubiquitin carrier protein ubc2,ubiquitin-protein ligase ubc2. Engineered: yes. Mutation: yes. E3 ubiquitin-protein ligase bre1. Chain: v, u.
Source:
Saccharomyces cerevisiae s288c. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: rad6, ubc2, ygl058w. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: bre1, ydl074c.
Resolution:
3.05Å
R-factor:
0.237
R-free:
0.279
Authors:
P.K.Shukla,M.B.Chandrasekharan
Key ref:
P.K.Shukla and m.b.chandrasekharan Rad6(p43l)-Bre1 complex.
To be published
, .
PubMed id:
36715322
Date:
29-Apr-22
Release date:
11-Jan-23
PROCHECK
Headers
References
Protein chain
?
P06104
(UBC2_YEAST) - Ubiquitin-conjugating enzyme E2 2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
172 a.a.
149 a.a.
*
Protein chains
?
Q07457
(BRE1_YEAST) - E3 ubiquitin-protein ligase BRE1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
700 a.a.
160 a.a.
Key:
PfamA domain
Secondary structure
*
PDB and UniProt seqs differ at 1 residue position (black cross)
Enzyme reactions
Enzyme class 2:
Chain A:
E.C.2.3.2.23
- E2 ubiquitin-conjugating enzyme.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Reaction:
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- cysteine
Enzyme class 3:
Chains V, U:
E.C.2.3.2.27
- RING-type E3 ubiquitin transferase.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Reaction:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N
6
- ubiquitinyl-[acceptor protein]-L-lysine
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
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