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1A0I

ATP-DEPENDENT DNA LIGASE FROM BACTERIOPHAGE T7 COMPLEX WITH ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003690molecular_functiondouble-stranded DNA binding
A0003909molecular_functionDNA ligase activity
A0003910molecular_functionDNA ligase (ATP) activity
A0005524molecular_functionATP binding
A0006260biological_processDNA replication
A0006266biological_processDNA ligation
A0006281biological_processDNA repair
A0006310biological_processDNA recombination
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP A 1
ChainResidue
AGLU32
ALYS222
ALYS232
ATRP236
ALYS238
AHOH351
AHOH434
AHOH459
AILE33
ALYS34
ATYR35
AARG39
AARG55
AGLU93
ATYR149
AILE220

Functional Information from PROSITE/UniProt
site_idPS00333
Number of Residues24
DetailsDNA_LIGASE_A2 ATP-dependent DNA ligase signature 2. EGLIVKdpmci...YKrgk...Ksgww.KMK
ChainResidueDetails
AGLU217-LYS240

site_idPS00697
Number of Residues9
DetailsDNA_LIGASE_A1 ATP-dependent DNA ligase AMP-binding site. EIKYDGVRG
ChainResidueDetails
AGLU32-GLY40

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: N6-AMP-lysine intermediate => ECO:0000255|PROSITE-ProRule:PRU10135
ChainResidueDetails
ALYS34

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:8653795
ChainResidueDetails
AGLU32
AARG39
AARG55
AGLU93
ALYS232

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU217

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:8653795
ChainResidueDetails
ALYS238

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 11106756, 1988940, 10656817
ChainResidueDetails
ALYS34
ALYS238
ALYS240

site_idMCSA1
Number of Residues3
DetailsM-CSA 202
ChainResidueDetails
ALYS34hydrogen bond donor, nucleofuge, nucleophile, polar interaction
ALYS238electrostatic stabiliser, hydrogen bond donor, steric role
ALYS240electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-07-10

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