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5L2X

Crystal structure of human PrimPol ternary complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003887molecular_functionDNA-directed DNA polymerase activity
A0003896molecular_functionDNA primase activity
A0006269biological_processDNA replication, synthesis of primer
A0042276biological_processerror-prone translesion synthesis
B0003887molecular_functionDNA-directed DNA polymerase activity
B0003896molecular_functionDNA primase activity
B0006269biological_processDNA replication, synthesis of primer
B0042276biological_processerror-prone translesion synthesis
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue DTP A 401
ChainResidue
AARG76
AARG291
ALYS297
ACA402
AHOH519
AHOH530
CDT3
DDDG14
ATYR100
AASP114
AGLU116
ALYS165
ASER167
AHIS169
AARG288
AASN289

site_idAC2
Number of Residues4
Detailsbinding site for residue CA A 402
ChainResidue
AASP114
AGLU116
ADTP401
AHOH514

site_idAC3
Number of Residues16
Detailsbinding site for residue DTP B 401
ChainResidue
BARG76
BTYR100
BASP114
BGLU116
BLYS165
BSER167
BHIS169
BARG288
BASN289
BARG291
BLYS297
BCA402
BHOH537
BHOH544
GDT3
HDDG14

site_idAC4
Number of Residues4
Detailsbinding site for residue CA B 402
ChainResidue
BASP114
BGLU116
BDTP401
BHOH503

site_idAC5
Number of Residues5
Detailsbinding site for Di-nucleotide DC G 6 and 5IU G 7
ChainResidue
GDG5
GDA8
HDT10
HDA11
HDG12

site_idAC6
Number of Residues6
Detailsbinding site for Di-nucleotide 5IU G 7 and DA G 8
ChainResidue
GDC6
GDC9
HDG9
HDT10
HDA11
HDG12

site_idAC7
Number of Residues6
Detailsbinding site for Di-nucleotide DC H 13 and DDG H 14
ChainResidue
BASP280
BARG288
BDTP401
GDC4
GDG5
HDG12

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:27819052, ECO:0007744|PDB:5L2X
ChainResidueDetails
AARG76
ALYS165
AARG288
ALYS297
BARG76
BLYS165
BARG288
BLYS297

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:24126761, ECO:0000305|PubMed:27819052, ECO:0007744|PDB:5L2X
ChainResidueDetails
AASP114
BASP114

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:27819052, ECO:0007744|PDB:5L2X
ChainResidueDetails
AGLU116
BGLU116

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER255
BSER255

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PDB entries from 2024-07-10

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