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4WS4

Crystal structure of Mycobacterium tuberculosis uracil-DNA glycosylase in complex with 5-nitrouracil, Form I

Functional Information from GO Data
ChainGOidnamespacecontents
A0004844molecular_functionuracil DNA N-glycosylase activity
A0005737cellular_componentcytoplasm
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0016787molecular_functionhydrolase activity
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
A0097510biological_processbase-excision repair, AP site formation via deaminated base removal
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue CIT A 301
ChainResidue
AASP58
AHOH490
ATHR72
APRO91
AARG92
ASER93
A5NU303
AHOH415
AHOH424
AHOH429

site_idAC2
Number of Residues9
Detailsbinding site for residue CIT A 302
ChainResidue
AGLN67
AGLY169
AARG170
ALEU195
AHOH402
AHOH417
AHOH419
AHOH476
AHOH583

site_idAC3
Number of Residues12
Detailsbinding site for residue 5NU A 303
ChainResidue
AGLN67
AASP68
ATYR70
ASER80
APHE81
ASER93
AASN127
AHIS191
ACIT301
AHOH567
AHOH590
AHOH698

site_idAC4
Number of Residues2
Detailsbinding site for residue IPA A 304
ChainResidue
AGLN120
AHOH712

site_idAC5
Number of Residues6
Detailsbinding site for residue DMS A 305
ChainResidue
AGLY39
AARG41
AGLY203
ASER204
AARG209
AHOH481

site_idAC6
Number of Residues5
Detailsbinding site for residue DMS A 306
ChainResidue
AILE36
AARG41
ATYR42
AGLU212
AHOH626

site_idAC7
Number of Residues5
Detailsbinding site for residue DMS A 307
ChainResidue
APRO89
ATRP90
AHOH604
AHOH605
AHOH618

site_idAC8
Number of Residues4
Detailsbinding site for residue DMS A 308
ChainResidue
ATHR54
APHE55
AHOH484
AHOH718

site_idAC9
Number of Residues4
Detailsbinding site for residue CL A 309
ChainResidue
AARG41
AARG133
AHOH468
AHOH584

site_idAD1
Number of Residues1
Detailsbinding site for residue CL A 310
ChainResidue
AARG40

Functional Information from PROSITE/UniProt
site_idPS00130
Number of Residues10
DetailsU_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. RVLIvGQDPY
ChainResidueDetails
AARG61-TYR70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AASP68

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PDB entries from 2024-07-17

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