acetylation and additional posttranslational modifications [20]. They estimated the
affinity limit of detection for this method to be ~0.5 mM, and thus weaker interactions may have been missed. Due to the limited information content from this assay,
these interactions should be further verified by additional biophysical methods, such
as ITC, which was carried out for a subset of these interactions in that report.
Table 1 Crystal structure information of human and nonhuman bromodomains
Bromodomain
a
Number of structures
Apo/holo PDB entry
Holo PDB entry
ASH1L
1
3mqm
NA
ATAD2A
43
4tu6
4tte
ATAD2B
1
3lxj
NA
BAZ1A
1
5uiy
NA
BAZ2B
268
5pen
5l8u
BPTF
4
3uv2
NA
BRD1
300
5pqi
5poa
BRD2(1)
19
NA
3yek
BRD2(2)
35
5ibn
5u6v
BRD3(1)
2
3s91
2le5
BRD3(2)
6
2oo1
3s92
BRD4(1)
157
3lyi
3mxf
BRD4(2)
20
NA
3oni
BRD7
2
NA
5mq1
BRD9
30
4yy4
5iy7
BRDT(1)
6
2rfj
4flp
BRDT(2)
1
2wp1
NA
BRPF1B
1
4lc2
NA
CECR2
2
3nxb
5v84
CREBBP
66
4ouf
5i89
EP300
4
NA
5nu5
GCN5L2
2
3d7c
5mlj
PB1(1)
1
3ui5
NA
PB1(5)
14
3g0j
5fh8
PCAF
18
3gg3
5lvq
PHIP(2)
8
3mb3
5enf
SMARCA4
4
2grc
5dkd
SP100
12
4ptb
5pwc
TAF1(2)
8
3uv4
5mg2
TAF1L(2)
2
3hmh
5igl
TRIM24
16
3o33
5h1t
TRIM33A
5
3u5m
5mr8
WDR9(1)
1
3qet
NA
ZMYND11
4
4ns5
NA
a Numbering in parenthesis indicates the order of the bromodomain from the N-terminus of the
protein. NA indicates the structure is not available. Current as of December 2018
296
W. C. K. Pomerantz et al.