Structure of PDB 4xnh Chain B

Receptor sequence

>4xnhB (length=197) Species: 4932 (Saccharomyces cerevisiae)

PINIRRATINDIICMQNANLHNLPENYMMKYYMYHILSWPEASFVATTTT
LDCEDRTIKLDPTYLAPGEKLVGYVLVKMNDDPNEPPNGHITSLSVMRTY
RRMGIAENLMRQALFALREVHQAEYVSLHVRQSNRAALHLYRDTLAFEVL
SIEKSYYQDGEDAYAMKKVLKLEELQISNFTHRREKLEDDLESDLLE

3D structure

• PDB: 4xnh Crystal structure of yeast N-terminal acetyltransferase NatE (IP6) in complex with a bisubstrate
• Chain: B
• Resolution: 2.1 Å

Enzymatic activity

• Enzyme Commision number: 2.3.1.255: N-terminal amino-acid N(alpha)-acetyltransferase NatA.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	peptide	B	E26 Y28 Y32 T116 Y180 Y181	E25 Y27 Y31 T92 Y156 Y157
BS02	IHP	B	K80 Y85 K91 T123 Y124	K59 Y64 K70 T99 Y100
BS03	CMC	B	L24 S117 L118 S119 V120 R125 R126 G128 A130 E131 H153 V154 A160 H163 Y165 T168 R207	L23 S93 L94 S95 V96 R101 R102 G104 A106 E107 H129 V130 A136 H139 Y141 T144 R183

Gene Ontology

Molecular Function

• GO:0004596 peptide alpha-N-acetyltransferase activity
• GO:0005515 protein binding
• GO:0016746 acyltransferase activity
• GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
• GO:0042802 identical protein binding
• GO:1990189 peptide-serine-alpha-N-acetyltransferase activity
• GO:1990190 peptide-glutamate-alpha-N-acetyltransferase activity

Biological Process

• GO:0006474 N-terminal protein amino acid acetylation

Cellular Component

• GO:0005737 cytoplasm
• GO:0031415 NatA complex

External links

• PDB: RCSB:4xnh, PDBe:4xnh, PDBj:4xnh
• PDBsum: 4xnh
• UniProt: P07347|ARD1_YEAST N-terminal acetyltransferase A complex catalytic subunit ARD1 (Gene Name=ARD1)