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PDBsum entry 3rtr

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protein metals Protein-protein interface(s) links
Ligase PDB id
3rtr

 

 

 

 

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Contents
Protein chains
353 a.a.
86 a.a.
317 a.a.
79 a.a.
81 a.a.
81 a.a.
Metals
_ZN ×12
PDB id:
3rtr
Name: Ligase
Title: A ring e3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-ring ligases
Structure: Cullin-1. Chain: a, c, e, g. Fragment: unp residues 411-776. Synonym: cul-1. Engineered: yes. Mutation: yes. E3 ubiquitin-protein ligase rbx1. Chain: b, d, f, h. Fragment: unp residues 5-108.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: cul1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: rbx1, rnf75, roc1. Expression_system_taxid: 562
Resolution:
3.21Å     R-factor:   0.238     R-free:   0.283
Authors: M.F.Calabrese,D.C.Scott,D.M.Duda,C.R.Grace,I.Kurinov,R.W.Kriwacki, B.A.Schulman
Key ref: M.F.Calabrese et al. (2011). A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. Nat Struct Biol, 18, 947-949. PubMed id: 21765416
Date:
03-May-11     Release date:   20-Jul-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q13616  (CUL1_HUMAN) -  Cullin-1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
776 a.a.
353 a.a.*
Protein chain
Pfam   ArchSchema ?
P62877  (RBX1_HUMAN) -  E3 ubiquitin-protein ligase RBX1 from Homo sapiens
Seq:
Struc:
108 a.a.
86 a.a.
Protein chain
Pfam   ArchSchema ?
Q13616  (CUL1_HUMAN) -  Cullin-1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
776 a.a.
317 a.a.*
Protein chain
Pfam   ArchSchema ?
P62877  (RBX1_HUMAN) -  E3 ubiquitin-protein ligase RBX1 from Homo sapiens
Seq:
Struc:
108 a.a.
79 a.a.
Protein chain
Pfam   ArchSchema ?
P62877  (RBX1_HUMAN) -  E3 ubiquitin-protein ligase RBX1 from Homo sapiens
Seq:
Struc:
108 a.a.
81 a.a.
Protein chain
Pfam   ArchSchema ?
P62877  (RBX1_HUMAN) -  E3 ubiquitin-protein ligase RBX1 from Homo sapiens
Seq:
Struc:
108 a.a.
81 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 8 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: Chains A, C, E, G: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: Chains B, D, F, H: 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
   Enzyme class 4: Chains B, D, F, H: E.C.2.3.2.32  - cullin-RING-type E3 NEDD8 transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: S-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]- L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine + N6-[NEDD8- protein]-yl-[cullin]-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.

 

 
Nat Struct Biol 18:947-949 (2011)
PubMed id: 21765416  
 
 
A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases.
M.F.Calabrese, D.C.Scott, D.M.Duda, C.R.Grace, I.Kurinov, R.W.Kriwacki, B.A.Schulman.
 
  ABSTRACT  
 
No abstract given.

 

 

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