6IMK

The crystal structure of AsfvLIG:CG complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003909	molecular_function	DNA ligase activity
A	0003910	molecular_function	DNA ligase (ATP) activity
A	0005524	molecular_function	ATP binding
A	0006260	biological_process	DNA replication
A	0006281	biological_process	DNA repair
A	0006310	biological_process	DNA recombination
A	0016874	molecular_function	ligase activity
A	0044423	cellular_component	virion component
A	0046872	molecular_function	metal ion binding
A	0051301	biological_process	cell division

Functional Information from PROSITE/UniProt

site_id	PS00333
Number of Residues	28
Details	DNA_LIGASE_A2 ATP-dependent DNA ligase signature 2. EGAIVRnangp...YEpgynnyHsahlaKLK

Chain	Residue	Details
A	GLU291-LYS318

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site_id	PS00697
Number of Residues	9
Details	DNA_LIGASE_A1 ATP-dependent DNA ligase AMP-binding site. QRKRNGVRA

Chain	Residue	Details
A	GLN149-ALA157

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: N6-AMP-lysine intermediate => ECO:0000255|PROSITE-ProRule:PRU10135

Chain	Residue	Details
A	LYS151

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:30674878

Chain	Residue	Details
A	GLN149
A	LYS151
A	GLU203
A	PHE232
A	ILE294
A	LYS316

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	GLU291

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site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Important for the catalytic efficiency => ECO:0000269|PubMed:30674878

Chain	Residue	Details
A	ASN153
A	LEU211
A	LEU402
A	GLN403

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