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6BKG

Human LigIV catalytic domain with bound DNA-adenylate intermediate in closed conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003909molecular_functionDNA ligase activity
A0003910molecular_functionDNA ligase (ATP) activity
A0005524molecular_functionATP binding
A0006281biological_processDNA repair
A0006310biological_processDNA recombination
A0051103biological_processDNA ligation involved in DNA repair
A0071897biological_processDNA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 701
ChainResidue
AVAL206
AASN209

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 702
ChainResidue
ATYR298
AASP300
AGLN301

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 703
ChainResidue
AHOH864
DDG5
AGLY509
AILE581
AHOH801
AHOH808

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO A 704
ChainResidue
AARG383
AGLU514
AASP517
ALEU518
AASP586
AHOH855

site_idAC5
Number of Residues13
Detailsbinding site for residue AMP D 101
ChainResidue
AGLU271
ATHR272
ALYS273
ALEU274
AARG278
AGLU331
APHE367
AMET430
ALYS432
ALYS449
ALYS451
DDG2
PHOH103

Functional Information from PROSITE/UniProt
site_idPS00333
Number of Residues25
DetailsDNA_LIGASE_A2 ATP-dependent DNA ligase signature 2. EGIMVKqplsi...YKpdk...RgegwlKIK
ChainResidueDetails
AGLU427-LYS451

site_idPS00697
Number of Residues9
DetailsDNA_LIGASE_A1 ATP-dependent DNA ligase AMP-binding site. ETKLDGERM
ChainResidueDetails
AGLU271-MET279

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: N6-AMP-lysine intermediate => ECO:0000255|PROSITE-ProRule:PRU10135, ECO:0000269|PubMed:23523427, ECO:0000269|PubMed:29980672, ECO:0007744|PDB:3W1B
ChainResidueDetails
ALYS273

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P18858
ChainResidueDetails
AGLU271

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:23523427, ECO:0007744|PDB:3W1G, ECO:0007744|PDB:3W5O
ChainResidueDetails
ATHR272
ALYS273
ALEU274
ALYS449
ALYS451

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:23523427, ECO:0007744|PDB:3W5O
ChainResidueDetails
AARG278
ALYS345
APHE367
ALYS432

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLU331
AGLU427

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PDB entries from 2024-07-17

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