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2CFM

ATP-DEPENDENT DNA LIGASE FROM PYROCOCCUS FURIOSUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003909molecular_functionDNA ligase activity
A0003910molecular_functionDNA ligase (ATP) activity
A0005524molecular_functionATP binding
A0006260biological_processDNA replication
A0006281biological_processDNA repair
A0006310biological_processDNA recombination
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0071897biological_processDNA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A1562
ChainResidue
AGLU299
AHOH2218
AHOH2253
AHOH2329
AHOH2330
AHOH2419
AHOH2450

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE AMP A1563
ChainResidue
AGLU247
AILE248
ALYS249
ATYR250
AARG254
AARG269
AGLU299
APHE339
AMSE401
ALYS403
ALYS420
AHOH2233
AHOH2253
AHOH2356
AHOH2447
AHOH2448
AHOH2449
AHOH2450
ALEU226
AALA227

Functional Information from PROSITE/UniProt
site_idPS00333
Number of Residues25
DetailsDNA_LIGASE_A2 ATP-dependent DNA ligase signature 2. EGLMAKrldav...YEpgnrg.Kkwl..KIK
ChainResidueDetails
AGLU398-LYS422

site_idPS00697
Number of Residues9
DetailsDNA_LIGASE_A1 ATP-dependent DNA ligase AMP-binding site. EIKYDGARV
ChainResidueDetails
AGLU247-VAL255

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: N6-AMP-lysine intermediate => ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000269|PubMed:16820169
ChainResidueDetails
ALYS249

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000269|PubMed:16820169, ECO:0007744|PDB:2CFM
ChainResidueDetails
AGLU247
AARG254
AARG269
AGLU299
APHE339
ALYS420

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00407
ChainResidueDetails
AARG414

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a0i
ChainResidueDetails
ALYS249

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PDB entries from 2024-07-24

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