Structure of PDB 5tao Chain A

Receptor sequence
>5taoA (length=356) Species: 309800 (Haloferax volcanii DS2) [Search protein sequence]
RHDREFVRTFFTSPTAVEDDSAKMLRRAAGLRGMQAPDVWVPDNEDATAP
SMRDEGAENIVEVISEQGAEFPGEIHPRMVWHRDSPETRYQGFQHMLDIT
DPERGAVEHIHGFVIPEVGGIDDWKKADEFFTIVEHEHGLDEGSLAMSVI
IESGEAELAMGDLRDEMGKPTNNLERLFLLVDGEVDYTKDMRAMTPTGEL
PAWPELRHNTSRGASAAGCVAVDGPYDDIRDVEGYRERMTDNQAKGMLGI
WSLTPGQVVEANTSPLPPKTGSWLLDLTADELREELLGLTSYVPSMDDIV
DSMEEFEAAKWDEATYQAAMTPISLFQDVYENRPDQHEELEERYGAGVVE
RAMEVG
3D structure
PDB5tao Crystal structures of a halophilic archaeal malate synthase from Haloferax volcanii and comparisons with isoforms A and G.
ChainA
Resolution2.1 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 2.3.3.9: malate synthase.
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 GLV A D52 R84 E158 G189 V191 D192 D46 R78 E152 G183 V185 D186
BS02 GLV A R89 D90 E161 D196 R83 D84 E155 D190
BS03 GLV A E51 D52 E123 D192 E45 D46 E117 D186
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004474 malate synthase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006097 glyoxylate cycle
GO:0006099 tricarboxylic acid cycle
GO:0006107 oxaloacetate metabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5tao, PDBe:5tao, PDBj:5tao
PDBsum5tao
PubMed
UniProtD4GTL2|ACEB_HALVD Malate synthase (Gene Name=aceB)

[Back to BioLiP]