3H7H

Crystal structure of the human transcription elongation factor DSIF, hSpt4/hSpt5 (176-273)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0000993	molecular_function	RNA polymerase II complex binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0006325	biological_process	chromatin organization
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006368	biological_process	transcription elongation by RNA polymerase II
A	0008270	molecular_function	zinc ion binding
A	0032044	cellular_component	DSIF complex
A	0032785	biological_process	negative regulation of DNA-templated transcription, elongation
A	0032786	biological_process	positive regulation of DNA-templated transcription, elongation
A	0034243	biological_process	regulation of transcription elongation by RNA polymerase II
A	0034244	biological_process	negative regulation of transcription elongation by RNA polymerase II
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046872	molecular_function	metal ion binding
A	0046982	molecular_function	protein heterodimerization activity
A	0140673	biological_process	transcription elongation-coupled chromatin remodeling
B	0006354	biological_process	DNA-templated transcription elongation
B	0006357	biological_process	regulation of transcription by RNA polymerase II
B	0032784	biological_process	regulation of DNA-templated transcription elongation
B	0140673	biological_process	transcription elongation-coupled chromatin remodeling

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BME A 118

Functional Information from SwissProt/UniProt

Chain	Residue	Details
A	CYS16-CYS36

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:28892040, ECO:0007744\|PDB:5OIK

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	ALA2