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5VZE

Post-catalytic complex of human Polymerase Mu (W434A) mutant with incoming UTP

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 Residues6
Detailsbinding site for residue MG A 501
ChainResidue
AASP330
AASP332
AASP418
AMG502
AUTP505
AGOA506

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 502
ChainResidue
AUTP505
AHOH710
AASP330
AASP332
AMG501

site_idAC3
Number of Residues7
Detailsbinding site for residue NA A 503
ChainResidue
ATHR241
AILE243
AVAL246
PDT3
PU5
PHOH102
PHOH108

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 504
ChainResidue
ALEU484
AGLU485
AHOH698
AHOH817

site_idAC5
Number of Residues24
Detailsbinding site for residue UTP A 505
ChainResidue
AGLY319
AGLY320
AARG323
ALYS325
AGLY328
AHIS329
AASP330
AASP332
AGLY433
AALA434
ATHR435
AGLY436
AMG501
AMG502
AGOA506
AHOH660
AHOH663
AHOH689
AHOH710
AHOH737
AHOH747
AHOH757
PDA4
TDA5

site_idAC6
Number of Residues9
Detailsbinding site for residue GOA A 506
ChainResidue
AHIS329
AASP330
AASP332
AASP418
AMG501
AUTP505
AHOH742
AHOH800
PDA4

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO A 507
ChainResidue
APRO190
ASER191
APRO192
AGLN198
AHOH707

site_idAC8
Number of Residues5
Detailsbinding site for residue MG T 101
ChainResidue
THOH207
THOH211
THOH219
THOH239
THOH240

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

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PDB entries from 2024-09-11

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