Structure of PDB 3oyz Chain A

Receptor sequence
>3oyzA (length=376) Species: 309800 (Haloferax volcanii DS2) [Search protein sequence]
RHDREFVRTFFTSPTAVEGEDDSAKMLRRAAGLRGMQAPDVWVPDNEDAT
APSMRDEGAENIVEVISEQGAEFPGEIHPRMVWHRDSPETRYQGFQHMLD
ITDPERGAVEHIHGFVIPEVGGIDDWKKADEFFTIVEHEHGLDEGSLAMS
VIIESGEAELAMGDLRDEMGKPTNNLERLFLLVDGEVDYTKDMRAMTPTG
ELPAWPELRHNTSRGASAAGCVAVDGPYDDIRDVEGYRERMTDNQAKGML
GIWSLTPGQVVEANTSPLPPKTGSWLLDADELREELLGLTSYVPSMDDIV
DSMEEFEAAKEAGRGAIAMTQSATIEKDRMWDEATYQAAMTPISLFQDVY
ENRPDQHEELEERYGAGVVERAMEVG
3D structure
PDB3oyz Crystal structures of a halophilic archaeal malate synthase from Haloferax volcanii and comparisons with isoforms A and G.
ChainA
Resolution1.95 Å
3D
structure
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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 ACO A F15 T16 S17 M30 R33 A53 P231 R236 W257 L259 P261 A363 M386 D388 F11 T12 S13 M26 R29 A49 P227 R232 W253 L255 P257 A316 M330 D332
BS02 PYR A E158 G189 V191 D192 P231 W257 E154 G185 V187 D188 P227 W253
BS03 MG A E158 D192 E154 D188
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3oyz, PDBe:3oyz, PDBj:3oyz
PDBsum3oyz
PubMed21569248
UniProtD4GTL2|ACEB_HALVD Malate synthase (Gene Name=aceB)

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