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5GG6

Crystal structure of Mycobacterium smegmatis MutT1 in complex with 8-oxo-dGTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0006260biological_processDNA replication
A0006281biological_processDNA repair
A0008413molecular_function8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity
A0016787molecular_functionhydrolase activity
A0044715molecular_function8-oxo-dGDP phosphatase activity
A0044716molecular_function8-oxo-GDP phosphatase activity
A0046872molecular_functionmetal ion binding
B0006260biological_processDNA replication
B0006281biological_processDNA repair
B0008413molecular_function8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity
B0016787molecular_functionhydrolase activity
B0044715molecular_function8-oxo-dGDP phosphatase activity
B0044716molecular_function8-oxo-GDP phosphatase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue 8DG A 401
ChainResidue
AARG55
AASP147
AASP148
AMG402
AHOH518
AHOH526
AHOH551
AHOH562
AHOH564
AHOH568
AHOH575
AARG57
AHOH582
AHOH594
AHOH617
AHOH686
ATYR58
ALYS65
ALYS67
ATYR101
ALYS108
AGLU127
ATYR145

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 402
ChainResidue
ALYS65
AGLU85
AGLU127
A8DG401
AHOH555
AHOH682

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 403
ChainResidue
AHIS170
AARG186

site_idAC4
Number of Residues5
Detailsbinding site for residue CL A 404
ChainResidue
AHIS88
AASP121
APHE122
ATRP133
AHOH775

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO A 405
ChainResidue
AASP215
AHIS220

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 406
ChainResidue
AGLN144
AARG149
AHOH504
AHOH511
AHOH662

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO A 407
ChainResidue
ATHR292
ATYR315
ALEU316
ASER317
AHOH593
AHOH696

site_idAC8
Number of Residues24
Detailsbinding site for residue 8DG B 401
ChainResidue
BARG55
BARG57
BTYR58
BLYS65
BLYS67
BTYR101
BLYS108
BGLU127
BTYR145
BASP147
BASP148
BMG402
BHOH531
BHOH541
BHOH542
BHOH549
BHOH552
BHOH555
BHOH563
BHOH588
BHOH611
BHOH616
BHOH631
BHOH684

site_idAC9
Number of Residues6
Detailsbinding site for residue MG B 402
ChainResidue
BLYS65
BGLU85
BGLU127
B8DG401
BHOH534
BHOH695

site_idAD1
Number of Residues2
Detailsbinding site for residue CL B 403
ChainResidue
BARG262
BPRO263

site_idAD2
Number of Residues2
Detailsbinding site for residue CL B 404
ChainResidue
BHIS170
BARG186

site_idAD3
Number of Residues5
Detailsbinding site for residue CL B 405
ChainResidue
BHIS88
BASP121
BPHE122
BTRP133
BHOH730

Functional Information from PROSITE/UniProt
site_idPS00893
Number of Residues22
DetailsNUDIX_BOX Nudix box signature. GkldqgEtepvAAaREIhEEtG
ChainResidueDetails
AGLY66-GLY87

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:28375146, ECO:0000269|PubMed:28705712
ChainResidueDetails
AARG55
BLYS65
BGLU81
BGLU85
BTYR101
BLYS108
BGLU127
BTYR145
ALYS65
AGLU81
AGLU85
ATYR101
ALYS108
AGLU127
ATYR145
BARG55

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:28375146
ChainResidueDetails
AASP60
BASP60

222415

PDB entries from 2024-07-10

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