2CNM

RimI - Ribosomal S18 N-alpha-protein acetyltransferase in complex with a bisubstrate inhibitor (Cterm-Arg-Arg-Phe-Tyr-Arg-Ala-N-alpha- acetyl-S-CoA).

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2 Family	N-acetyltransferase NAT	8100307	4001800	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Acyl-CoA N-acyltransferases (Nat)	8100308	3000403	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8100308	3000403	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8100308	3000403	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	Acetyltransf_10_6	e2cnmB1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_10_6	ECOD (1.6)
C	Acetyltransf_10_6	e2cnmC1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_10_6	ECOD (1.6)
A	Acetyltransf_10_6	e2cnmA1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_10_6	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
C	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
A	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF00583	Acetyltransferase (GNAT) family (Acetyltransf_1)	Acetyltransferase (GNAT) family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	MODIFICATION OF 30S RIBOSOMAL SUBUNIT PROTEIN S18	acetyltransferase activity N-acetyltransferase activity acyltransferase activity peptide alpha-N-acetyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity peptide N-acetyltransferase activity peptide-alanine-alpha-N-acetyltransferase activity catalytic activity N-acyltransferase activity	-	intracellular anatomical structure cytoplasm cellular anatomical entity
D, E, F	30S RIBOSOMAL PROTEIN S18	RNA binding small ribosomal subunit rRNA binding binding organic cyclic compound binding rRNA binding nucleic acid binding structural molecule activity structural constituent of ribosome	organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process primary metabolic process translation gene expression macromolecule biosynthetic process organic substance metabolic process biosynthetic process organic substance biosynthetic process metabolic process cellular process protein metabolic process organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process primary metabolic process translation gene expression macromolecule biosynthetic process organic substance metabolic process biosynthetic process organic substance biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process	cytosolic small ribosomal subunit protein-containing complex intracellular anatomical structure small ribosomal subunit cellular anatomical entity intracellular organelle ribosomal subunit cytosolic ribosome organelle ribonucleoprotein complex intracellular non-membrane-bounded organelle ribosome cytoplasm cytosol cytosolic small ribosomal subunit protein-containing complex intracellular anatomical structure small ribosomal subunit cellular anatomical entity intracellular organelle ribosomal subunit cytosolic ribosome organelle ribonucleoprotein complex intracellular non-membrane-bounded organelle ribosome cytoplasm cytosol non-membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR043690	N-acetyltransferase RimI	Family
A, B, C	IPR006464	N-acetyltransferase RimI/Ard1	Family
A, B, C	IPR016181	Acyl-CoA N-acyltransferase	Homologous Superfamily
A, B, C	IPR000182	GNAT domain	Domain
D, E, F	IPR001648	Small ribosomal subunit protein bS18	Family
D, E, F	IPR018275	Small ribosomal subunit protein bS18, conserved site	Conserved Site
D, E, F	IPR036870	Small ribosomal subunit protein bS18 superfamily	Homologous Superfamily

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
D, E, F	ACE	RESID: AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 PSI-MOD : N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.