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6H2U

Crystal structure of human METTL5-TRMT112 complex, the 18S rRNA m6A1832 methyltransferase at 1.6A 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
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue SAM A 301
ChainResidue
APHE19
AGLY61
ACYS62
AVAL64
AASP81
AILE82
ACYS107
AASP108
AVAL109
AASN126
APRO128
ALEU26
AHOH416
AHOH455
AHOH521
AGLU27
AGLN28
ATYR29
APRO30
ATHR31
AGLY59
ACYS60

site_idAC2
Number of Residues7
Detailsbinding site for residue EDO A 302
ChainResidue
AVAL54
ASER119
AARG150
AHOH408
BLEU8
BMET45
BLYS48

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 303
ChainResidue
ASER113
AASN114
AMET116
ASER117
AGLU147

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO A 304
ChainResidue
ATHR46
ATYR47
AHOH402
AHOH449
AHOH470
BHOH334

site_idAC5
Number of Residues8
Detailsbinding site for residue SO4 A 305
ChainResidue
ATHR151
AARG206
ASER208
AHIS211
AHOH407
AHOH421
AHOH433
AHOH459

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 A 306
ChainResidue
ALYS175
AHIS210
AHIS211

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO B 201
ChainResidue
BARG14
BVAL49
BGLU50
BTRP51
BSER52

site_idAC8
Number of Residues9
Detailsbinding site for residue EDO B 202
ChainResidue
BHIS12
BVAL13
BARG14
BSER18
BARG19
BGLY20
BHOH308
BHOH355
BHOH375

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 Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:31328227, ECO:0007744|PDB:6H2U, ECO:0007744|PDB:6H2V
ChainResidueDetails
AASP81
AASP108
AGLN28
ATHR31
AGLY59

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:31328227, ECO:0007744|PDB:6H2U
ChainResidueDetails
ACYS62

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:31328227, ECO:0007744|PDB:6H2V
ChainResidueDetails
AVAL64

219869

PDB entries from 2024-05-15

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