Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4QZB

Mouse Tdt in complex with a DSB substrate, C-T base pair

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
AASP343
AASP345
ADCT603
AHOH892

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 602
ChainResidue
ATHR253
AVAL255
AVAL258
UDA5
UHOH106

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE DCT A 603
ChainResidue
AGLY332
AGLY333
AARG336
ALYS338
AGLY341
AHIS342
AASP343
AASP345
AGLY449
ATRP450
AGLY452
AARG454
AGLU457
AMG601
AHOH707
AHOH760
AHOH819
AHOH861
AHOH892
TDG6
TDT7
UDC6

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 Residues3
DetailsBINDING: BINDING => ECO:0000305, ECO:0007744|PDB:4I2B, ECO:0007744|PDB:4I2C, ECO:0007744|PDB:4I2D, ECO:0007744|PDB:4I2E
ChainResidueDetails
AGLY333
AHIS342
AGLY449

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305, ECO:0007744|PDB:1JMS, ECO:0007744|PDB:4I2B
ChainResidueDetails
AASP345
AASP434
AASP343

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER134

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 632
ChainResidueDetails
AASP345metal ligand
AASP434metal ligand, proton acceptor, proton donor
AASP343metal ligand

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon