Structure of PDB 3oce Chain B

Receptor sequence
>3oceB (length=461) Species: 359391 (Brucella abortus 2308) [Search protein sequence]
MTRREQDSLGERDIPMDAYFGIQTLRAVENFSLSDVALNHIPALVRALAM
VKKAAATANYKLRQLPEPKYAAIVAACDDIIDGLLMEQFVVDVFQGGAGT
SSNMNANEVIANRALEHLGRPRGDYQTIHPNDDVNMSQSTNDVYPTAVRL
ALLLSQNQVQTALHRLIAAFEAKGREFATVIKIGRTQLQDAVPITLGQEF
EAFAATLREDTARLEEVAALFREVNLGGTAIGTRINASHAYAEQAIVELS
QISGIELKATGNLVEASWDTGAFVTFSGILRRIAVKLSKIANDLRLLSSG
PRSGLGEIRLPAVQPGSSIMPGKVNPVIPESVNQVCYQVIGNDLTVTMAA
ESGQLQLNAFEPLIVYNILSSMRLLGRAMTNLAERCVDGIEANVERCRAG
AEESISLATALVPVVGYARAAEIAKQALASGQTVMEVAISKGLDASALTI
MLDPLRMAFPP
3D structure
PDB3oce Crystal structure of fumarate lyase:delta crystallin from Brucella melitensis bound to cobalt
ChainB
Resolution2.58 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q187 S317 K323 E330
Catalytic site (residue number reindexed from 1) Q187 S317 K323 E330
Enzyme Commision number 4.3.1.1: aspartate ammonia-lyase.
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 CO B E265 D269 E265 D269
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008797 aspartate ammonia-lyase activity
GO:0016829 lyase activity
Biological Process
GO:0006099 tricarboxylic acid cycle
GO:0006531 aspartate metabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3oce, PDBe:3oce, PDBj:3oce
PDBsum3oce
PubMed
UniProtQ2YLW1

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