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6IMK

The crystal structure of AsfvLIG:CG complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003909molecular_functionDNA ligase activity
A0003910molecular_functionDNA ligase (ATP) activity
A0005524molecular_functionATP binding
A0006260biological_processDNA replication
A0006281biological_processDNA repair
A0006310biological_processDNA recombination
A0006974biological_processDNA damage response
A0016874molecular_functionligase activity
A0044423cellular_componentvirion component
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
Functional Information from PROSITE/UniProt
site_idPS00333
Number of Residues28
DetailsDNA_LIGASE_A2 ATP-dependent DNA ligase signature 2. EGAIVRnangp...YEpgynnyHsahlaKLK
ChainResidueDetails
AGLU291-LYS318

site_idPS00697
Number of Residues9
DetailsDNA_LIGASE_A1 ATP-dependent DNA ligase AMP-binding site. QRKRNGVRA
ChainResidueDetails
AGLN149-ALA157

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues196
DetailsRegion: {"description":"AD domain","evidences":[{"source":"PubMed","id":"30674878","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"N6-AMP-lysine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10135","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30674878","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Important for the catalytic efficiency","evidences":[{"source":"PubMed","id":"30674878","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-09-24

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