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PDBsum entry 8ieg

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protein dna_rna metals Protein-protein interface(s) links
Nuclear protein PDB id
8ieg

 

 

 

 

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Contents
Protein chains
98 a.a.
80 a.a.
109 a.a.
94 a.a.
64 a.a.
148 a.a.
DNA/RNA
Metals
_ZN ×4
PDB id:
8ieg
Name: Nuclear protein
Title: Bre1(mrbd-ring)/rad6-ub/nucleosome complex
Structure: Histone h3.1. Chain: k, e. Synonym: histone h3/a,histone h3/b,histone h3/c,histone h3/d,histone h3/f,histone h3/h,histone h3/i,histone h3/j,histone h3/k,histone h3/l. Engineered: yes. Histone h4. Chain: l, f. Engineered: yes.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: h3c1, h3fa, hist1h3a, h3c2, h3fl, hist1h3b, h3c3, h3fc hist1h3c, h3c4, h3fb, hist1h3d, h3c6, h3fd, hist1h3e, h3c7, h3fi, hist1h3f, h3c8, h3fh, hist1h3g, h3c10, h3fk, hist1h3h, h3c11, h3ff, hist1h3i, h3c12, h3fj, hist1h3j. Expressed in: escherichia coli. Expression_system_taxid: 562.
Authors: H.Ai,Z.Deng,M.Pan,L.Liu
Key ref: Z.Deng et al. Mechanistic insights into nucleosomal h2b monoubiquit mediated by yeast bre1-Rad6 and its human homolog rnf20/rnf40-Hrad6a.. Mol cell, . PubMed id: 37633270
Date:
15-Feb-23     Release date:   06-Sep-23    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
P68431  (H31_HUMAN) -  Histone H3.1 from Homo sapiens
Seq:
Struc:
136 a.a.
98 a.a.
Protein chains
P62805  (H4_HUMAN) -  Histone H4 from Homo sapiens
Seq:
Struc:
103 a.a.
80 a.a.
Protein chains
P04908  (H2A1B_HUMAN) -  Histone H2A type 1-B/E from Homo sapiens
Seq:
Struc:
130 a.a.
109 a.a.
Protein chains
O60814  (H2B1K_HUMAN) -  Histone H2B type 1-K from Homo sapiens
Seq:
Struc:
126 a.a.
94 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.
64 a.a.
Protein chain
P06104  (UBC2_YEAST) -  Ubiquitin-conjugating enzyme E2 2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
172 a.a.
148 a.a.
Key:    Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

DNA/RNA chains
  A-C-A-G-G-A-T-G-T-A-T-A-T-A-T-C-T-G-A-C-A-C-G-T-G-C-C-T-G-G-A-G-A-C-T-A-G-G-G- 147 bases
  C-T-G-G-A-G-A-A-T-C-C-C-G-G-T-G-C-C-G-A-G-G-C-C-G-C-T-C-A-A-T-T-G-G-T-C-G-T-A- 147 bases

 Enzyme reactions 
   Enzyme class 2: Chains A, B: 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 3: Chain R: 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
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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