1PJR

STRUCTURE OF DNA HELICASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000725	biological_process	recombinational repair
A	0003677	molecular_function	DNA binding
A	0003678	molecular_function	DNA helicase activity
A	0004386	molecular_function	helicase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006259	biological_process	DNA metabolic process
A	0006260	biological_process	DNA replication
A	0009314	biological_process	response to radiation
A	0016787	molecular_function	hydrolase activity
A	0016853	molecular_function	isomerase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0032991	cellular_component	protein-containing complex
A	0033202	cellular_component	DNA helicase complex
A	0043138	molecular_function	3'-5' DNA helicase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00560","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10388562","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10388562","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1qhg

Chain	Residue	Details
A	GLU224
A	LYS37
A	ARG610

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site_id	MCSA1
Number of Residues	6
Details	M-CSA 833

Chain	Residue	Details
A	LYS37	electrostatic stabiliser
A	THR38	metal ligand
A	ASP223	electrostatic stabiliser
A	GLU224	proton acceptor
A	GLN254	electrostatic stabiliser
A	ARG610	electrostatic stabiliser

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