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PDBe Entry: 1c4z 
STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY
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LIGASE
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X-RAY DIFFRACTION
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Resolution: 2.6 Å, R-factor: 26.2%, Free R-factor: 29.0%, Spacegroup: P 21 21 21
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17/11/1999, deposition: 14/10/1999, last revision: 24/02/2009
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Huang, L. ; Kinnucan, E. ; Wang, G. ; Beaudenon, S. ; Howley, P.M. ; Huibregtse, J.M. ; Pavletich, N.P.
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Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. SCIENCE vol:286, pag:1321-1326 (1999) [PubMed ID 10558980 ]
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BILOBAL STRUCTURE , ELONGATED SHAPE , E3 UBIQUITIN LIGASE , E2 UBIQUITIN CONJUGATING ENZYME
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6.3.2.19 ExPASy BRENDA (D)
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Homo sapiens(human) 9606 (A B C D)
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Ubiquitin-protein ligase E3A (EC 6.3.2.-) (E6AP ubiquitin-protein ligase) (Oncogenic protein-associated protein E6-AP) (Human papillomavirus E6-associated protein) (Renal carcinoma antigen NY-REN-54) Q05086 (A B C) Ubiquitin-conjugating enzyme E2 L3 (EC 6.3.2.19) (Ubiquitin-protein ligase L3) (Ubiquitin carrier protein L3) (UbcH7) (E2-F1) (L-UBC) P68036 (D)
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A, B, C, D
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1ubq, 1d5f
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| A, B, C |
UBIQUITIN-PROTEIN LIGASE E3A |
Protein |
Q05086 (UBE3A_HUMAN)
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358 |
97% |
| D |
UBIQUITIN CONJUGATING ENZYME E2 |
Protein |
P68036 (UB2L3_HUMAN)
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154 |
93% |
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