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PDBsum entry 5af6

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protein metals Protein-protein interface(s) links
Signaling protein PDB id
5af6

 

 

 

 

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Contents
Protein chains
76 a.a.
28 a.a.
29 a.a.
28 a.a.
27 a.a.
Metals
_ZN ×5
PDB id:
5af6
Name: Signaling protein
Title: Structure of lys33-linked diub bound to trabid nzf1
Structure: Ubiquitin. Chain: a, b, c, d, e. Engineered: yes. Mutation: yes. Other_details: isopeptide bonds across between chains, a76 c and d33 nz, b76 c and a33 nz, c76c and b33 nz, e76 c and c33 nz. Isopeptide bond across the asu for, d76 c and e33 nz symm. Trabid. Chain: f, g, h, i, j.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosettaii.
Resolution:
3.40Å     R-factor:   0.182     R-free:   0.222
Authors: M.A.Michel,P.R.Elliott,K.N.Swatek,M.Simicek,J.N.Pruneda,J.L.Wagstaff, S.M.V.Freund,D.Komander
Key ref: M.A.Michel et al. (2015). Assembly and specific recognition of k29- and k33-linked polyubiquitin. Mol Cell, 58, 95. PubMed id: 25752577 DOI: 10.1016/j.molcel.2015.01.042
Date:
19-Jan-15     Release date:   25-Mar-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0CG48  (UBC_HUMAN) -  Polyubiquitin-C from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
685 a.a.
76 a.a.*
Protein chains
Pfam   ArchSchema ?
Q9UGI0  (ZRAN1_HUMAN) -  Ubiquitin thioesterase ZRANB1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
708 a.a.
28 a.a.
Protein chain
Pfam   ArchSchema ?
Q9UGI0  (ZRAN1_HUMAN) -  Ubiquitin thioesterase ZRANB1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
708 a.a.
29 a.a.
Protein chain
Pfam   ArchSchema ?
Q9UGI0  (ZRAN1_HUMAN) -  Ubiquitin thioesterase ZRANB1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
708 a.a.
28 a.a.
Protein chain
Pfam   ArchSchema ?
Q9UGI0  (ZRAN1_HUMAN) -  Ubiquitin thioesterase ZRANB1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
708 a.a.
27 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, B, C, D, E: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: Chains F, G, H, I, J: E.C.3.4.19.12  - ubiquitinyl hydrolase 1.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Thiol-dependent hydrolysis of ester, thiolester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
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: 10.1016/j.molcel.2015.01.042 Mol Cell 58:95 (2015)
PubMed id: 25752577  
 
 
Assembly and specific recognition of k29- and k33-linked polyubiquitin.
M.A.Michel, P.R.Elliott, K.N.Swatek, M.Simicek, J.N.Pruneda, J.L.Wagstaff, S.M.Freund, D.Komander.
 
  ABSTRACT  
 
No abstract given.

 

 

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