CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.920 | Histone Acetyltransferase; Chain A |
|
1.20.920.10 | Bromodomain-like |
Domain Context
CATH Clusters
| Superfamily | Bromodomain-like |
| Functional Family | Histone acetyltransferase KAT2B |
Enzyme Information
| 2.3.1.48 |
Histone acetyltransferase.
based on mapping to UniProt Q92831
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine.
-!- A group of enzymes acetylating histones. -!- Several of the enzymes can also acetylate lysines in other proteins.
|
| 2.3.1.57 |
Diamine N-acetyltransferase.
based on mapping to UniProt Q92831
Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine.
-!- Acts on 1,3-diaminopropane, 1,5-diaminopentane, putrescine, spermidine (forming N(1)- and N(8)-acetylspermidine), spermine, N(1)- acetylspermidine and N(8)-acetylspermidine.
|
UniProtKB Entries (2)
| Q92831 |
KAT2B_HUMAN
Homo sapiens
Histone acetyltransferase KAT2B
|
| P61830 |
H3_YEAST
Saccharomyces cerevisiae S288C
Histone H3
|
PDB Structure
| PDB | 2RNW |
| External Links | |
| Method | SOLUTION NMR |
| Organism | Escherichia |
| Primary Citation |
Structural Basis of Site-Specific Histone Recognition by the Bromodomains of Human Coactivators PCAF and CBP/p300
Structure
|
