Structure of PDB 1tuy Chain A

Receptor sequence

>1tuyA (length=399) Species: 2210 (Methanosarcina thermophila)

MKVLVINAGSSSLKYQLIDMTNESALAVGLCERIGIDNSIITQKKFDGKK
LEKLTDLPTHKDALEEVVKALTDDEFGVIKDMGEINAVGHRVVHGGEKFT
TSALYDEGVEKAIKDCFELAPLHNPPNMMGISACAEIMPGTPMVIVFDTA
FHQTMPPYAYMYALPYDLYEKHGVRKYGFHGTSHKYVAERAALMLGKPAE
ETKIITCHLGNGSSITAVEGGKSVETSMGFTPLEGLAMGTRCGSIDPAIV
PFLMEKEGLTTREIDTLMNKKSGVLGVSGLSNDFRDLDEAASKGNRKAEL
ALEIFAYKVKKFIGEYSAVLNGADAVVFTAGIGENSASIRKRILTGLDGI
GIKIDDEKNKIRGQEIDISTPDAKVRVFVIPTNEELAIARETKEIVETE

3D structure

• PDB: 1tuy Structural and Kinetic Analyses of Arginine Residues in the Active Site of the Acetate Kinase from Methanosarcina thermophila.
• Chain: A
• Resolution: 3.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N7 R91 H180 R241 E384
• Catalytic site (residue number reindexed from 1): N7 R91 H180 R241 E384
• Enzyme Commision number: 2.7.2.1: acetate 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	SO4	A	R91 H123 H180 G212	R91 H123 H180 G212
BS02	ADP	A	K14 G210 N211 D283 F284 R285 G331 I332 N335	K14 G210 N211 D283 F284 R285 G331 I332 N335

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0005524 ATP binding
• GO:0008776 acetate kinase activity
• GO:0016301 kinase activity
• GO:0016774 phosphotransferase activity, carboxyl group as acceptor
• GO:0046872 metal ion binding

Biological Process

• GO:0006082 organic acid metabolic process
• GO:0006083 acetate metabolic process
• GO:0006085 acetyl-CoA biosynthetic process
• GO:0016310 phosphorylation

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1tuy, PDBe:1tuy, PDBj:1tuy
• PDBsum: 1tuy
• PubMed: 15647264
• UniProt: P38502|ACKA_METTE Acetate kinase (Gene Name=ackA)