Structure of PDB 1tuy Chain B

Receptor sequence
>1tuyB (length=398) Species: 2210 (Methanosarcina thermophila) [Search protein sequence]
MKVLVINAGSSSLKYQLIDMTNESALAVGLCERIGIDNSIITQKKFDGKK
LEKLTDLPTHKDALEEVVKALTDDEFGVIKDMGEINAVGHRVVHGGEKFT
TSALYDEGVEKAIKDCFELAPLHNPPNMMGISACAEIMPGTPMVIVFDTA
FHQTMPPYAYMYALPYDLYEKHGVRKYGFHGTSHKYVAERAALMLGKPAE
ETKIITCHLGNGSSITAVEGGKSVETSMGFTPLEGLAMGTRCGSIDPAIV
PFLMEKEGLTTREIDTLMNKKSGVLGVSGLSNDFRDLDEAASKGNRKAEL
ALEIFAYKVKKFIGEYSAVLNGADAVVFTAGIGENSASIRKRILTGLDGI
GIKIDDEKNKIRGQEIDISTPDAKVRVFVIPTNEELAIARETKEIVET
3D structure
PDB1tuy Structural and Kinetic Analyses of Arginine Residues in the Active Site of the Acetate Kinase from Methanosarcina thermophila.
ChainB
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 ADP B G210 N211 F284 R285 A330 G331 I332 N335 G210 N211 F284 R285 A330 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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1tuy, PDBe:1tuy, PDBj:1tuy
PDBsum1tuy
PubMed15647264
UniProtP38502|ACKA_METTE Acetate kinase (Gene Name=ackA)

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