2XYI

Crystal Structure of Nurf55 in complex with a H4 peptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0000976	molecular_function	transcription cis-regulatory region binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005667	cellular_component	transcription regulator complex
A	0005700	cellular_component	polytene chromosome
A	0006325	biological_process	chromatin organization
A	0006335	biological_process	DNA replication-dependent chromatin assembly
A	0006338	biological_process	chromatin remodeling
A	0006355	biological_process	regulation of DNA-templated transcription
A	0007307	biological_process	eggshell chorion gene amplification
A	0007346	biological_process	regulation of mitotic cell cycle
A	0007379	biological_process	segment specification
A	0016581	cellular_component	NuRD complex
A	0016589	cellular_component	NURF complex
A	0031491	molecular_function	nucleosome binding
A	0031507	biological_process	heterochromatin formation
A	0031523	cellular_component	Myb complex
A	0033186	cellular_component	CAF-1 complex
A	0034728	biological_process	nucleosome organization
A	0035097	cellular_component	histone methyltransferase complex
A	0035098	cellular_component	ESC/E(Z) complex
A	0042393	molecular_function	histone binding
A	0042803	molecular_function	protein homodimerization activity
A	0042826	molecular_function	histone deacetylase binding
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0045893	biological_process	positive regulation of DNA-templated transcription
A	0070822	cellular_component	Sin3-type complex
A	0090575	cellular_component	RNA polymerase II transcription regulator complex
A	0140718	biological_process	facultative heterochromatin formation
B	0046982	molecular_function	protein heterodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PG4 A 1416

Chain	Residue
A	TYR185
A	HOH2391
A	ASP202
A	GLU235
A	ASP252
A	PHE325
A	HOH2225
A	HOH2263
A	HOH2264
A	HOH2390

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PEG A 1417

Chain	Residue
A	HOH2136

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PG4 A 1418

Chain	Residue
A	LYS313
A	HIS315
A	SER316
A	GLU318

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PG4 A 1419

Chain	Residue
A	HIS240
A	HIS243
A	GLU290
A	PHE291
A	LEU307
A	HOH2393

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site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 1420

Chain	Residue
A	LEU314
A	HOH2358

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Functional Information from PROSITE/UniProt

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSAsdDhTICLWDI

Chain	Residue	Details
A	LEU197-ILE211
A	LEU293-LEU307
A	LEU337-LEU351

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:22389435

Chain	Residue	Details
B	LYS31

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:18327897

Chain	Residue	Details
A	SER100

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