Structure of PDB 4xpd Chain A

Receptor sequence
>4xpdA (length=774) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
DQFLEALKLYEGKQYKKSLKLLDAILKKDGSHVDSLALKGLDLYSVGEKD
DAASYVANAIRKISPICCHVLGIYMRNTKEYKESIKWFTAALNNGSTNKQ
IYRDLATLQSQIGDFKNALVSRKKYWEAFLGYRANWTSLAVAQDVNGERQ
QAINTLSQFEKLAEGKISDSEKYEHSECLMYKNDIMYKAASDNQDKLQNV
LKHLNDIEPCVFDKFGLLERKATIYMKLGQLKDASIVYRTLIKRNPDNFK
YYKLLEVSLGIQGDNKLKKALYGKLEQFYPRCEPPKFIPLTFLQDKEELS
KKLREYVLPQLERGVPATFSNVKPLYQRRKSKVSPLLEKIVLDYLSGLDP
TQDPIPFIWTNYYLSQHFLFLKDFPKAQEYIDAALDHTPTLVEFYILKAR
ILKHLGLMDTAAGILEEGRQLDLQDRFINCKTVKYFLRANNIDKAVEVAS
LFTKNDDSVNGIKDLHLVEASWFIVEQAEAYYRLYLDRKKKLDDLASLKK
QIANDIKENQWLVRKYKGLALKRFNAIPKFYKQFEDDQLDFHSYCMRKGT
PRAYLEMLEWGKALYTKPMYVRAMKEASKLYFQMHDDRLKKRKETEAKSV
AAYPSDQDNDVFGEKLIETSTPMEDFATEFYNNYSMQVREDERDYILDFE
FNYRIGKLALCFASLNKFAKRFGTTSGLFGSMAIVLLHATRNDTPFVVTK
SLEKEYSENFPLNEFDWLNFYQEKFGKNDINGLLFLYRYRDDVPIGSSNL
KEMIISSLSPLEPHSQNEILQYYL
3D structure
PDB4xpd Crystal structure of yeast N-terminal acetyltransferase NatE (ppGpp) in complex with a bisubstrate
ChainA
Resolution2.81 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number ?
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 G4P A K349 Q353 R426 K429 K457 K460 K323 Q327 R400 K403 K431 K434
Gene Ontology
Molecular Function
GO:0004596 peptide alpha-N-acetyltransferase activity
GO:0005515 protein binding
GO:0043022 ribosome binding
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0031415 NatA complex

View graph for
Molecular Function

View graph for
Cellular Component
External links
PDB RCSB:4xpd, PDBe:4xpd, PDBj:4xpd
PDBsum4xpd
PubMed
UniProtP12945|NAT1_YEAST N-terminal acetyltransferase A complex subunit NAT1 (Gene Name=NAT1)

[Back to BioLiP]