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6H2V

Crystal structure of human METTL5-TRMT112 complex, the 18S rRNA m6A1832 methyltransferase at 2.5A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0001650cellular_componentfibrillar center
A0003676molecular_functionnucleic acid binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005730cellular_componentnucleolus
A0005829cellular_componentcytosol
A0006364biological_processrRNA processing
A0008168molecular_functionmethyltransferase activity
A0008988molecular_functionrRNA (adenine-N6-)-methyltransferase activity
A0031167biological_processrRNA methylation
A0032259biological_processmethylation
A0042995cellular_componentcell projection
A0045202cellular_componentsynapse
A0045727biological_processpositive regulation of translation
A0048863biological_processstem cell differentiation
A0098793cellular_componentpresynapse
A0098794cellular_componentpostsynapse
A1904047molecular_functionS-adenosyl-L-methionine binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006364biological_processrRNA processing
B0008276molecular_functionprotein methyltransferase activity
B0018364biological_processpeptidyl-glutamine methylation
B0030488biological_processtRNA methylation
B0031167biological_processrRNA methylation
B0032991cellular_componentprotein-containing complex
B0045815biological_processtranscription initiation-coupled chromatin remodeling
B0046982molecular_functionprotein heterodimerization activity
B0048471cellular_componentperinuclear region of cytoplasm
B0070476biological_processrRNA (guanine-N7)-methylation
B0141106molecular_functiontRNA methyltransferase activator activity
B2000234biological_processpositive regulation of rRNA processing
C0001650cellular_componentfibrillar center
C0003676molecular_functionnucleic acid binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005730cellular_componentnucleolus
C0005829cellular_componentcytosol
C0006364biological_processrRNA processing
C0008168molecular_functionmethyltransferase activity
C0008988molecular_functionrRNA (adenine-N6-)-methyltransferase activity
C0031167biological_processrRNA methylation
C0032259biological_processmethylation
C0042995cellular_componentcell projection
C0045202cellular_componentsynapse
C0045727biological_processpositive regulation of translation
C0048863biological_processstem cell differentiation
C0098793cellular_componentpresynapse
C0098794cellular_componentpostsynapse
C1904047molecular_functionS-adenosyl-L-methionine binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006364biological_processrRNA processing
D0008276molecular_functionprotein methyltransferase activity
D0018364biological_processpeptidyl-glutamine methylation
D0030488biological_processtRNA methylation
D0031167biological_processrRNA methylation
D0032991cellular_componentprotein-containing complex
D0045815biological_processtranscription initiation-coupled chromatin remodeling
D0046982molecular_functionprotein heterodimerization activity
D0048471cellular_componentperinuclear region of cytoplasm
D0070476biological_processrRNA (guanine-N7)-methylation
D0141106molecular_functiontRNA methyltransferase activator activity
D2000234biological_processpositive regulation of rRNA processing
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue SAM A 301
ChainResidue
APHE19
AGLY61
ACYS62
AVAL64
AASP81
AILE82
ACYS107
AASP108
AVAL109
AASN126
APRO128
ALEU26
AHOH401
AGLU27
AGLN28
ATYR29
APRO30
ATHR31
AGLY59
ACYS60

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 302
ChainResidue
ATHR151
ALYS175
AARG206
ASER208
AHIS211

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 303
ChainResidue
ALYS175
AHIS210
AHIS211

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 304
ChainResidue
AARG32
APRO187
AALA188

site_idAC5
Number of Residues6
Detailsbinding site for residue PEG B 201
ChainResidue
AGLU84
AGLN106
BPRO108
BSER110
BILE113
BASN115

site_idAC6
Number of Residues1
Detailsbinding site for residue EDO B 202
ChainResidue
BGLU90

site_idAC7
Number of Residues3
Detailsbinding site for residue SO4 B 203
ChainResidue
BGLU36
BPHE37
BARG82

site_idAC8
Number of Residues20
Detailsbinding site for residue SAM C 301
ChainResidue
CPHE19
CLEU26
CGLU27
CGLN28
CTYR29
CPRO30
CTHR31
CGLY59
CCYS60
CGLY61
CCYS62
CVAL64
CASP81
CILE82
CCYS107
CASP108
CVAL109
CASN126
CPRO128
CHOH401

site_idAC9
Number of Residues5
Detailsbinding site for residue PG0 C 302
ChainResidue
ALYS132
AASN133
CARG32
CPRO33
CHIS34

site_idAD1
Number of Residues4
Detailsbinding site for residue SO4 C 303
ChainResidue
CTHR151
CARG206
CSER208
CHIS211

site_idAD2
Number of Residues3
Detailsbinding site for residue SO4 C 304
ChainResidue
CLYS175
CHIS210
CHIS211

site_idAD3
Number of Residues8
Detailsbinding site for residue EDO D 201
ChainResidue
CASN91
CASP103
CMET104
DCME33
DGLU92
DARG111
DGLY112
DPG0202

site_idAD4
Number of Residues8
Detailsbinding site for residue PG0 D 202
ChainResidue
CGLU95
DGLU29
DARG31
DCME33
DILE94
DGLU95
DARG111
DEDO201

site_idAD5
Number of Residues3
Detailsbinding site for residue SO4 D 203
ChainResidue
BARG62
DPHE37
DARG82

Functional Information from PROSITE/UniProt
site_idPS00092
Number of Residues7
DetailsN6_MTASE N-6 Adenine-specific DNA methylases signature. VIMNPPF
ChainResidueDetails
AVAL123-PHE129

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231
ChainResidueDetails
BSER119
CASP108
DSER119
AGLY59
AASP81
AASP108
CGLN28
CTHR31
CGLY59
CASP81

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
BSER125
DSER125

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:31328227, ECO:0007744|PDB:6H2V
ChainResidueDetails
AVAL64
CVAL64

219140

PDB entries from 2024-05-01

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