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PDBsum entry 4whv

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protein metals Protein-protein interface(s) links
Ligase/protein binding PDB id
4whv

 

 

 

 

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Contents
Protein chains
147 a.a.
136 a.a.
101 a.a.
71 a.a.
Metals
_ZN ×8
PDB id:
4whv
Name: Ligase/protein binding
Title: E3 ubiquitin-protein ligase rnf8 in complex with ubiquitin-conjugating enzyme e2 n and polyubiquitin-b
Structure: Ubiquitin-conjugating enzyme e2 n. Chain: b, e, h, k. Fragment: unp residues 1-152. Synonym: bendless-like ubiquitin-conjugating enzyme,ubc13,ubch13, ubiquitin carrier protein n,ubiquitin-protein ligase n. Engineered: yes. Mutation: yes. E3 ubiquitin-protein ligase rnf8. Chain: c, d, i, j.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ube2n, blu. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: rnf8, kiaa0646. Gene: ubb. Expression_system_taxid: 562.
Resolution:
8.30Å     R-factor:   0.330     R-free:   0.337
Authors: C.D.Hodge,R.A.Edwards,J.N.M.Glover
Key ref: C.D.Hodge et al. (2016). RNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity That Is Essential for DNA Double Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment. J Biol Chem, 291, 9396-9410. PubMed id: 26903517 DOI: 10.1074/jbc.M116.715698
Date:
23-Sep-14     Release date:   30-Sep-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P61088  (UBE2N_HUMAN) -  Ubiquitin-conjugating enzyme E2 N from Homo sapiens
Seq:
Struc:
152 a.a.
147 a.a.*
Protein chains
Pfam   ArchSchema ?
O76064  (RNF8_HUMAN) -  E3 ubiquitin-protein ligase RNF8 from Homo sapiens
Seq:
Struc:
485 a.a.
136 a.a.
Protein chains
Pfam   ArchSchema ?
O76064  (RNF8_HUMAN) -  E3 ubiquitin-protein ligase RNF8 from Homo sapiens
Seq:
Struc:
485 a.a.
101 a.a.
Protein chains
Pfam   ArchSchema ?
P0CG47  (UBB_HUMAN) -  Polyubiquitin-B from Homo sapiens
Seq:
Struc:
229 a.a.
71 a.a.
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 2: Chains A, F, G, L: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: Chains B, E, H, K: 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 4: Chains C, D, I, J: 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 + N6- 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.

 

 
DOI no: 10.1074/jbc.M116.715698 J Biol Chem 291:9396-9410 (2016)
PubMed id: 26903517  
 
 
RNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity That Is Essential for DNA Double Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment.
C.D.Hodge, I.H.Ismail, R.A.Edwards, G.L.Hura, A.T.Xiao, J.A.Tainer, M.J.Hendzel, J.N.Glover.
 
  ABSTRACT  
 
No abstract given.

 

 

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