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6WIC

Pre-catalytic quaternary complex of human Polymerase Mu on a complementary DNA double-strand break substrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0005634cellular_componentnucleus
A0006281biological_processDNA repair
A0016779molecular_functionnucleotidyltransferase activity
A0034061molecular_functionDNA polymerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues29
Detailsbinding site for residue DUP A 701
ChainResidue
AGLY319
ATRP434
AGLY436
ALYS438
AMG702
AMG703
AHOH870
AHOH889
AHOH912
AHOH917
AHOH924
AGLY320
AHOH934
AHOH935
AHOH949
AHOH954
AHOH965
AHOH998
AHOH1025
PDA4
PHOH103
TDA5
AARG323
ALYS325
AGLY328
AHIS329
AASP330
AASP332
AGLY433

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 702
ChainResidue
AASP330
AASP332
ADUP701
AMG703
AHOH917

site_idAC3
Number of Residues7
Detailsbinding site for residue MG A 703
ChainResidue
AASP330
AASP332
AASP418
ADUP701
AMG702
PDA4
PHOH103

site_idAC4
Number of Residues6
Detailsbinding site for residue NA A 704
ChainResidue
ATHR241
AILE243
AVAL246
AHOH1026
PDT3
PHOH115

site_idAC5
Number of Residues6
Detailsbinding site for residue K A 705
ChainResidue
ATHR241
AILE243
AVAL246
AHOH1026
PDT3
PHOH115

site_idAC6
Number of Residues5
Detailsbinding site for residue CL A 706
ChainResidue
AARG387
AARG445
ASER458
TDT6
UDA1

site_idAC7
Number of Residues9
Detailsbinding site for residue GOL A 707
ChainResidue
ASER425
AGLN426
AHIS459
AGLY460
APHE469
AGLN471
AHOH802
AHOH865
AHOH866

site_idAC8
Number of Residues3
Detailsbinding site for residue PEG A 708
ChainResidue
AGLN426
AHIS459
AHOH832

site_idAC9
Number of Residues3
Detailsbinding site for residue 1PE A 709
ChainResidue
AARG253
AARG256
AGLU451

Functional Information from PROSITE/UniProt
site_idPS00522
Number of Residues20
DetailsDNA_POLYMERASE_X DNA polymerase family X signature. GGFrRGklqGhDVDFLIthP
ChainResidueDetails
AGLY319-PRO338

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP330
AASP332
AASP418

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Responsible for the low discrimination between dNTP and rNTP
ChainResidueDetails
AGLY433

237992

PDB entries from 2025-06-25

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