Structure of PDB 3oce Chain B Binding Site BS01

Receptor Information

>3oce Chain B (length=461) Species: 359391 (Brucella abortus 2308)

MTRREQDSLGERDIPMDAYFGIQTLRAVENFSLSDVALNHIPALVRALAM
VKKAAATANYKLRQLPEPKYAAIVAACDDIIDGLLMEQFVVDVFQGGAGT
SSNMNANEVIANRALEHLGRPRGDYQTIHPNDDVNMSQSTNDVYPTAVRL
ALLLSQNQVQTALHRLIAAFEAKGREFATVIKIGRTQLQDAVPITLGQEF
EAFAATLREDTARLEEVAALFREVNLGGTAIGTRINASHAYAEQAIVELS
QISGIELKATGNLVEASWDTGAFVTFSGILRRIAVKLSKIANDLRLLSSG
PRSGLGEIRLPAVQPGSSIMPGKVNPVIPESVNQVCYQVIGNDLTVTMAA
ESGQLQLNAFEPLIVYNILSSMRLLGRAMTNLAERCVDGIEANVERCRAG
AEESISLATALVPVVGYARAAEIAKQALASGQTVMEVAISKGLDASALTI
MLDPLRMAFPP

Ligand information

• Ligand ID: CO
• InChI: InChI=1S/Co/q+2
• InChIKey: XLJKHNWPARRRJB-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Co+2]
  CACTVS 3.341: [Co++]
• Formula: Co
• Name: COBALT (II) ION
• DrugBank: DB14205
• PDB chain: 3oce Chain B Residue 471

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3oce Crystal structure of fumarate lyase:delta crystallin from Brucella melitensis bound to cobalt
• Resolution: 2.58 Å
• Binding residue (original residue number in PDB): E265 D269
• Binding residue (residue number reindexed from 1): E265 D269
• Annotation score: 1

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.

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

External links

• PDB: RCSB:3oce, PDBe:3oce, PDBj:3oce
• PDBsum: 3oce
• UniProt: Q2YLW1