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PDBsum entry 5ulh

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
5ulh

 

 

 

 

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Contents
Protein chains
148 a.a.
75 a.a.
51 a.a.
Ligands
GOL ×2
SCN ×2
Metals
_ZN ×2
Waters ×68
PDB id:
5ulh
Name: Transferase
Title: Structure of rnf165 in complex with a ubch5b~ub conjugate
Structure: Ubiquitin-conjugating enzyme e2 d2. Chain: a. Synonym: (e3-independent) e2 ubiquitin-conjugating enzyme d2,e2 ubiquitin-conjugating enzyme d2,ubiquitin carrier protein d2, ubiquitin-conjugating enzyme e2(17)kb 2,ubiquitin-conjugating enzyme e2-17 kda 2,ubiquitin-protein ligase d2,p53-regulated ubiquitin- conjugating enzyme 1. Engineered: yes. Mutation: yes.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ube2d2, pubc1, ubc4, ubc5b, ubch4, ubch5b. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_cell_line: bl21. Gene: ubb. Gene: rnf165.
Resolution:
1.95Å     R-factor:   0.190     R-free:   0.217
Authors: A.J.Middleton,C.L.Day,J.D.Wright
Key ref: A.J.Middleton et al. Discovery of new non-Covalent ubiquitin binding sites ubch5. To be published, .
Date:
24-Jan-17     Release date:   07-Jun-17    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P62837  (UB2D2_HUMAN) -  Ubiquitin-conjugating enzyme E2 D2 from Homo sapiens
Seq:
Struc:
147 a.a.
148 a.a.*
Protein chain
Pfam   ArchSchema ?
P0CG47  (UBB_HUMAN) -  Polyubiquitin-B from Homo sapiens
Seq:
Struc:
229 a.a.
75 a.a.
Protein chain
Pfam   ArchSchema ?
Q6ZSG1  (RN165_HUMAN) -  E3 ubiquitin-protein ligase ARK2C from Homo sapiens
Seq:
Struc:
346 a.a.
51 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: 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 2: Chain A: E.C.2.3.2.24  - (E3-independent) E2 ubiquitin-conjugating enzyme.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6- monoubiquitinyl-[acceptor protein]-L-lysine
   Enzyme class 3: Chain B: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 4: Chain C: 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.

 

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