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6GO5

TdT chimera (Loop1 of pol mu) - Ternary complex with 1-nt gapped DNA substrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0006281biological_processDNA repair
A0016779molecular_functionnucleotidyltransferase activity
A0034061molecular_functionDNA polymerase activity
B0003677molecular_functionDNA binding
B0003887molecular_functionDNA-directed DNA polymerase activity
B0006281biological_processDNA repair
B0016779molecular_functionnucleotidyltransferase activity
B0034061molecular_functionDNA polymerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue NA A 601
ChainResidue
ATHR253
AVAL255
AVAL258
FDT5

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 602
ChainResidue
AASP343
AASP345
AXC5603

site_idAC3
Number of Residues17
Detailsbinding site for residue XC5 A 603
ChainResidue
AARG336
ALYS338
AGLY341
AHIS342
AASP343
AASP345
ATRP451
ATHR452
AGLY453
AARG455
AMG602
AHOH734
AHOH743
FDG6
HDG6
AGLY332
AGLY333

site_idAC4
Number of Residues4
Detailsbinding site for residue MG B 601
ChainResidue
BASP343
BASP345
BXC5603
BHOH756

site_idAC5
Number of Residues6
Detailsbinding site for residue NA B 602
ChainResidue
BTHR253
BVAL255
BVAL258
BHOH782
LDT5
LHOH102

site_idAC6
Number of Residues17
Detailsbinding site for residue XC5 B 603
ChainResidue
BGLY332
BGLY333
BARG336
BLYS338
BGLY341
BHIS342
BASP343
BASP345
BTRP451
BTHR452
BGLY453
BGLU458
BMG601
BHOH718
BHOH760
LDG6
NDG6

Functional Information from PROSITE/UniProt
site_idPS00522
Number of Residues20
DetailsDNA_POLYMERASE_X DNA polymerase family X signature. GGFrRGkmtGhDVDFLItsP
ChainResidueDetails
AGLY332-PRO351

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsRegion: {"description":"Involved in DNA binding","evidences":[{"source":"PubMed","id":"11823435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23856622","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4I2B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I2C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I2D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I2E","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues18
DetailsRegion: {"description":"Involved in ssDNA binding"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Responsible for the low discrimination between dNTP and rNTP","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 632
ChainResidueDetails
AASP343metal ligand
AASP345metal ligand
AASP435metal ligand, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 632
ChainResidueDetails
BASP343metal ligand
BASP345metal ligand
BASP435metal ligand, proton acceptor, proton donor

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PDB entries from 2025-12-17

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