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1VLR

Crystal structure of mRNA decapping enzyme (DcpS) from Mus musculus at 1.83 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000288biological_processnuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
A0000290biological_processdeadenylation-dependent decapping of nuclear-transcribed mRNA
A0000340molecular_functionRNA 7-methylguanosine cap binding
A0000932cellular_componentP-body
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006397biological_processmRNA processing
A0008380biological_processRNA splicing
A0016787molecular_functionhydrolase activity
A0042802molecular_functionidentical protein binding
A0045292biological_processmRNA cis splicing, via spliceosome
A0110156biological_processmRNA methylguanosine-cap decapping
A0140932molecular_function5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity
B0000288biological_processnuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
B0000290biological_processdeadenylation-dependent decapping of nuclear-transcribed mRNA
B0000340molecular_functionRNA 7-methylguanosine cap binding
B0000932cellular_componentP-body
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006397biological_processmRNA processing
B0008380biological_processRNA splicing
B0016787molecular_functionhydrolase activity
B0042802molecular_functionidentical protein binding
B0045292biological_processmRNA cis splicing, via spliceosome
B0110156biological_processmRNA methylguanosine-cap decapping
B0140932molecular_function5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 339
ChainResidue
BGLY45
BARG47
BLYS66
BVAL67
BGLU69
BGLU235
BHOH565

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 339
ChainResidue
AGLU249
AALA250
ALYS253
AHOH568
APHE190
AGLU246

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 340
ChainResidue
AGLY76

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 341
ChainResidue
AGLN299
AHOH630
BASN303
BHIS310
BARG314
BTHR315
BLEU316
BHOH701

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 342
ChainResidue
AASN303
AHIS310
AARG314
ATHR315
ALEU316
AHOH373
AHOH497
BGLN299

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 340
ChainResidue
AHOH444
BPRO119
BPRO120
BARG121
BSER124

Functional Information from PROSITE/UniProt
site_idPS00892
Number of Residues19
DetailsHIT_1 HIT domain signature. RvylhYlPsYyHLHVHFTA
ChainResidueDetails
AARG263-ALA281

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AHIS276
BHIS276

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATRP174
AGLU184
AASP204
ALYS206
BLYS206
BHIS267
AHIS267
BTRP174
BGLU184
BASP204

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:Q96C86
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q96C86
ChainResidueDetails
ASER23
BSER23

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER100
BSER100

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS137
BLYS137

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q96C86
ChainResidueDetails
ALYS141
BLYS141

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PDB entries from 2024-06-12

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