STRUCTURAL BIOLOGY & CHEMICAL EVIDENCEDataset v1.2 · Phase 6D · Comparative experimental recognition environments

Experimental structure

2X4W

Molecular basis of Histone H3K36me3 recognition by the PWWP domain of BRPF1.

Complexes PWWP coordinates observed X-RAY DIFFRACTION

Original coordinates

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PDB deposition
2X4W Deposited model
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Original coordinates are available from a locally verified historical archive or the bundled source and load on request.

Coordinate coverage

Mapped chains

1 chain / domain rows

Label and author chain identifiers are kept separately. Observed Cα counts refer to each mapped annotation core.

ProteinLabel chainAuthor chainDomainObserved Cα / coreObserved substitutions
BRPF1A["A"]UP:P55201:PWWP184 / 840

Chemical identity

Chemical components and interpretation

2 component records
CCDNameRoleFull InChIKey
FMTFORMIC ACIDbuffer/additive
incidental
BDAGIHXWWSANSR-UHFFFAOYSA-N
HOHWATERsolvent
incidental
XLYOFNOQVPJJNP-UHFFFAOYSA-N

Geometry, with defined scope

Independent contact evidence

Inspect 2 retained contact records
CCD / instanceProtein chainContact classMinimum core / broader domain distance Å
FMT · CBRPF1 · Anative annotation core contact2.48 / 2.48
M3L · BBRPF1 · Anative annotation core contact2.81 / 2.81

Biological partners

HISTONE H3.2 · histone or histone peptide · label chains ["B"]

Source interpretation

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This entry was included in all-entry coordinate/contact calculations but not in the 36-entry focused structural sample.