Structure of PDB 4xpd Chain B

Receptor sequence

>4xpdB (length=187) Species: 4932 (Saccharomyces cerevisiae)

PINIRRATINDIICMQNANLHNLPENYMMKYYMYHILSWPEASFVATTTT
LDPTYLAPGEKLVGYVLVKMNDDQNEPPNGHITSLSVMRTYRRMGIAENL
MRQALFALREVHQAEYVSLHVRQSNRAALHLYRDTLAFEVLSIEKSYYQD
GEDAYAMKKVLKLEELQISNFTHRRKLEDDLESDLLE

3D structure

• PDB: 4xpd Crystal structure of yeast N-terminal acetyltransferase NatE (ppGpp) in complex with a bisubstrate
• Chain: B
• Resolution: 2.81 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 T83 Y147 Y148
BS02	G4P	B	P83 Y85 K91	P53 Y55 K61
BS03	CMC	B	L24 S117 L118 S119 V120 R125 R126 M127 G128 A130 H153 V154 N158 A160 A161 H163 Y165 T168	L23 S84 L85 S86 V87 R92 R93 M94 G95 A97 H120 V121 N125 A127 A128 H130 Y132 T135

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