Structure of PDB 3ju5 Chain A

Receptor sequence
>3ju5A (length=363) Species: 307972 (Apostichopus japonicus) [Search protein sequence]
ANLNQKKYPAKDDFPNFEGHKSLLSKYLTADMYAKLRDVATPSGYTLDRA
IQNGVDNPDFHLGLLAGDEETYTVFADLFDPVIEEYHNGFKKTDNHKTDL
DASKILDDVLDPAYVISSRVRTGRNIRGMALSPHVCRSERRAIEKMVSEA
LNSLAADLKGKYYSLMKMDEKTQQQLIDDHFLFDRPVSRHFTSGGMARDF
PDGRGIWHNDKKNFLVWINEEDHTRIISMQMGGNMKEVFERFTRGLTEVE
KHIKDKTGKEFMKNDHLGFVLTCPSNLGTGVRCSVHAKLPHMAKDKRFEE
ICTKMRLQKRGTSVGGVYDISNLDRLGSSEVEQVNCVIKGVKVLIEMEKK
LEKGESIDDLVPK
3D structure
PDB3ju5 Structural basis for a reciprocating mechanism of negative cooperativity in dimeric phosphagen kinase activity
ChainA
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) R122 E222 R226 C274 S276 R283 R311
Catalytic site (residue number reindexed from 1) R121 E221 R225 C273 S275 R282 R310
Enzyme Commision number 2.7.3.3: arginine kinase.
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 MG A A2 R50 A1 R49
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004054 arginine kinase activity
GO:0004111 creatine kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016772 transferase activity, transferring phosphorus-containing groups
Biological Process
GO:0016310 phosphorylation
GO:0046314 phosphocreatine biosynthetic process
Cellular Component
GO:0005739 mitochondrion

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3ju5, PDBe:3ju5, PDBj:3ju5
PDBsum3ju5
PubMed19783784
UniProtQ9XY07|KARG_STIJA Arginine kinase (Gene Name=AK)

[Back to BioLiP]