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4FZV

Crystal structure of the human MTERF4:NSUN4:SAM ternary complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000957biological_processmitochondrial RNA catabolic process
A0001510biological_processRNA methylation
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005762cellular_componentmitochondrial large ribosomal subunit
A0006364biological_processrRNA processing
A0006396biological_processRNA processing
A0008168molecular_functionmethyltransferase activity
A0008173molecular_functionRNA methyltransferase activity
A0008649molecular_functionrRNA methyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0009383molecular_functionrRNA (cytosine-C5-)-methyltransferase activity
A0016428molecular_functiontRNA (cytidine-5-)-methyltransferase activity
A0019843molecular_functionrRNA binding
A0031167biological_processrRNA methylation
A0032259biological_processmethylation
A0042254biological_processribosome biogenesis
A0062152molecular_functionmRNA (cytidine-5-)-methyltransferase activity
A1900864biological_processmitochondrial RNA modification
B0003690molecular_functiondouble-stranded DNA binding
B0006355biological_processregulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE SAM A 401
ChainResidue
ALEU180
ALEU205
ASER206
AARG209
AASP237
AGLY238
AASP255
AVAL256
APRO257
AHOH503
AHOH584
ACYS181
AHOH610
AHOH685
AHOH700
AHOH773
AALA182
AALA183
APRO185
AGLY185
AGLY186
ALYS187
AASP204

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 402
ChainResidue
ALEU312
AASN317
AGLU318
AHOH605

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 403
ChainResidue
AGLN290

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01023, ECO:0000269|PubMed:22949673
ChainResidueDetails
ACYS310

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ACYS181

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01023, ECO:0000269|PubMed:23022348
ChainResidueDetails
AASP237
AASP255

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER206

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PDB entries from 2024-11-06

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