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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
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
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
A0016740molecular_functiontransferase activity
A0019843molecular_functionrRNA binding
A0031167biological_processrRNA methylation
A0032259biological_processmethylation
A0042254biological_processribosome biogenesis
A0062152molecular_functionmRNA (cytidine-5-)-methyltransferase activity
A1900864biological_processmitochondrial RNA modification
A1902775biological_processmitochondrial large ribosomal subunit assembly
A1990400molecular_functionmitochondrial ribosomal large subunit rRNA binding
B0003676molecular_functionnucleic acid binding
B0043231cellular_componentintracellular membrane-bounded organelle
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
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01023","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22949673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23022348","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22949673","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4FP9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22949673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23022348","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4FP9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FZV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01023","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22949673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23022348","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4FP9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FZV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01023","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues30
DetailsRepeat: {"description":"MTERF 1","evidences":[{"source":"PubMed","id":"23022348","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues27
DetailsRepeat: {"description":"MTERF 2","evidences":[{"source":"PubMed","id":"23022348","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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