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6BRH

The SAM domain of mouse SAMHD1 is critical for its activation and regulation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000724biological_processdouble-strand break repair via homologous recombination
A0003676molecular_functionnucleic acid binding
A0003697molecular_functionsingle-stranded DNA binding
A0003723molecular_functionRNA binding
A0004540molecular_functionRNA nuclease activity
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0005886cellular_componentplasma membrane
A0006203biological_processdGTP catabolic process
A0006260biological_processDNA replication
A0006281biological_processDNA repair
A0006974biological_processDNA damage response
A0008270molecular_functionzinc ion binding
A0008832molecular_functiondGTPase activity
A0009264biological_processdeoxyribonucleotide catabolic process
A0016446biological_processsomatic hypermutation of immunoglobulin genes
A0016787molecular_functionhydrolase activity
A0016793molecular_functiontriphosphoric monoester hydrolase activity
A0032567molecular_functiondGTP binding
A0035861cellular_componentsite of double-strand break
A0042802molecular_functionidentical protein binding
A0045087biological_processinnate immune response
A0045088biological_processregulation of innate immune response
A0046061biological_processdATP catabolic process
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
A0051607biological_processdefense response to virus
A0060339biological_processnegative regulation of type I interferon-mediated signaling pathway
A0097197cellular_componenttetraspanin-enriched microdomain
A0106375molecular_functiondeoxynucleoside triphosphate hydrolase activity
A0110025biological_processDNA strand resection involved in replication fork processing
B0000724biological_processdouble-strand break repair via homologous recombination
B0003676molecular_functionnucleic acid binding
B0003697molecular_functionsingle-stranded DNA binding
B0003723molecular_functionRNA binding
B0004540molecular_functionRNA nuclease activity
B0005525molecular_functionGTP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0005886cellular_componentplasma membrane
B0006203biological_processdGTP catabolic process
B0006260biological_processDNA replication
B0006281biological_processDNA repair
B0006974biological_processDNA damage response
B0008270molecular_functionzinc ion binding
B0008832molecular_functiondGTPase activity
B0009264biological_processdeoxyribonucleotide catabolic process
B0016446biological_processsomatic hypermutation of immunoglobulin genes
B0016787molecular_functionhydrolase activity
B0016793molecular_functiontriphosphoric monoester hydrolase activity
B0032567molecular_functiondGTP binding
B0035861cellular_componentsite of double-strand break
B0042802molecular_functionidentical protein binding
B0045087biological_processinnate immune response
B0045088biological_processregulation of innate immune response
B0046061biological_processdATP catabolic process
B0046872molecular_functionmetal ion binding
B0051289biological_processprotein homotetramerization
B0051607biological_processdefense response to virus
B0060339biological_processnegative regulation of type I interferon-mediated signaling pathway
B0097197cellular_componenttetraspanin-enriched microdomain
B0106375molecular_functiondeoxynucleoside triphosphate hydrolase activity
B0110025biological_processDNA strand resection involved in replication fork processing
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 701
ChainResidue
AARG196
AHIS199
AHIS238
AASP239
AASP343
AHOH804

site_idAC2
Number of Residues13
Detailsbinding site for residue DGT A 702
ChainResidue
APHE150
AASP169
AGLN174
AARG177
APHE197
BTYR187
BVAL188
BLYS420
BILE421
BARG494
AARG75
ALYS148
AVAL149

site_idAC3
Number of Residues13
Detailsbinding site for residue DGT B 701
ChainResidue
ATYR187
AVAL188
ALYS420
AILE421
AARG494
BARG75
BLYS148
BVAL149
BPHE150
BASP169
BGLN174
BARG177
BPHE197

site_idAC4
Number of Residues6
Detailsbinding site for residue MG B 702
ChainResidue
BARG196
BHIS199
BHIS238
BASP239
BASP343
BHOH801

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q9Y3Z3
ChainResidueDetails
AHIS265
BHIS265

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: in other chain => ECO:0000305|PubMed:29379009, ECO:0007744|PDB:6BRH
ChainResidueDetails
ALYS148
AASP169
BLYS148
BASP169

site_idSWS_FT_FI3
Number of Residues22
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9Y3Z3
ChainResidueDetails
AASN151
AHIS419
ALYS498
BASN151
BGLN181
BARG196
BHIS242
BASP341
BTYR347
BASP351
BARG409
AGLN181
BHIS413
BHIS419
BLYS498
AARG196
AHIS242
AASP341
ATYR347
AASP351
AARG409
AHIS413

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305|PubMed:29379009, ECO:0007744|PDB:6BRH
ChainResidueDetails
AHIS199
BASP343
BLYS420
BARG494
AHIS238
AASP239
AASP343
ALYS420
AARG494
BHIS199
BHIS238
BASP239

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:Q9Y3Z3
ChainResidueDetails
AARG365
AARG395
AASN401
ALYS565
BARG365
BARG395
BASN401
BLYS565

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER49
BSER49

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079
ChainResidueDetails
ATHR52
BTHR52

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER55
BSER55

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ATHR56
BTHR56

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Y3Z3
ChainResidueDetails
ASER64
ASER125
BSER64
BSER125

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:26667483, ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079
ChainResidueDetails
ATHR634
BTHR634

site_idSWS_FT_FI12
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:Q9Y3Z3
ChainResidueDetails
ALYS509
BLYS509

224201

PDB entries from 2024-08-28

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