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5D46

Structural Basis for a New Templated Activity by Terminal Deoxynucleotidyl Transferase: Implications for V(D)J Recombination

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
APOP603
CDC7

site_idAC2
Number of Residues4
Detailsbinding site for residue NA A 602
ChainResidue
ATHR253
AVAL255
AVAL258
CDT5

site_idAC3
Number of Residues10
Detailsbinding site for residue POP A 603
ChainResidue
AGLY333
AARG336
ALYS338
AGLY341
AHIS342
AASP343
AASP345
AMG601
CDC7
AGLY332

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 604
ChainResidue
AASP298
AGLY425
ALYS426
ATRP428

site_idAC5
Number of Residues1
Detailsbinding site for residue SO4 A 605
ChainResidue
AARG480

site_idAC6
Number of Residues5
Detailsbinding site for residue ACT A 606
ChainResidue
AASN184
AGLY186
ASER187
AHOH704
AHOH715

site_idAC7
Number of Residues3
Detailsbinding site for residue ACT A 607
ChainResidue
ALYS338
AMET339
ATHR340

site_idAC8
Number of Residues1
Detailsbinding site for residue ACT A 608
ChainResidue
AGLY213

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

225946

PDB entries from 2024-10-09

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