Structure of PDB 1g99 Chain B

Receptor sequence
>1g99B (length=398) Species: 2210 (Methanosarcina thermophila) [Search protein sequence]
MKVLVINAGSSSLKYQLIDMTNESALAVGLCERIGIDNSIITQKKFDGKK
LEKLTDLPTHKDALEEVVKALTDDEFGVIKDMGEINAVGHRVVHGGEKFT
TSALYDEGVEKAIKDCFELAPLHNPPNMMGISACAEIMPGTPMVIVFDTA
FHQTMPPYAYMYALPYDLYEKHGVRKYGFHGTSHKYVAERAALMLGKPAE
ETKIITCHLGNGSSITAVEGGKSVETSMGFTPLEGLAMGTRCGSIDPAIV
PFLMEKEGLTTREIDTLMNKKSGVLGVSGLSNDFRDLDEAASKGNRKAEL
ALEIFAYKVKKFIGEYSAVLNGADAVVFTAGIGENSASIRKRILTGLDGI
GIKIDDEKNKIRGQEIDISTPDAKVRVFVIPTNEELAIARETKEIVET
3D structure
PDB1g99 Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases.
ChainB
Resolution2.5 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 D283 F284 R285 G331 I332 N335 S336 G210 N211 D283 F284 R285 G331 I332 N335 S336
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:1g99, PDBe:1g99, PDBj:1g99
PDBsum1g99
PubMed11133963
UniProtP38502|ACKA_METTE Acetate kinase (Gene Name=ackA)

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