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4QZI

Mouse Tdt, F401A mutant, in complex with a DSB substrate and Zn2+

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 Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
AASP343
AASP345
AASP434
AMG603
UDA5
UDC6

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 602
ChainResidue
AASP473
AHIS475

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 603
ChainResidue
AASP345
AZN601
ADCT605
AHOH722
UDC6
AASP343

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 604
ChainResidue
ATHR253
AVAL255
AVAL258
UDA4

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE DCT A 605
ChainResidue
AGLY332
AGLY333
AARG336
ALYS338
AGLY341
AHIS342
AASP343
AASP345
AMG603
AHOH737
AHOH761
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
AASP343
AASP345
AASP434

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
AASP343metal ligand
AASP345metal ligand
AASP434metal ligand, proton acceptor, proton donor

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PDB entries from 2024-07-24

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