Structure of PDB 1sjb Chain B Binding Site BS01

Receptor Information

>1sjb Chain B (length=368) Species: 37632 (Amycolatopsis sp.)

MKLSGVELRRVQMPLVAPFRTSFGTQSVRELLLLRAVTPAGEGWGECVTM
AGPLYSSEYNDGAEHVLRHYLIPALLAAEDITAAKVTPLLAKFKGHRMAK
GALEMAVLDAELRAHERSFAAELGSVRDSVPCGVSVGIMDTIPQLLDVVG
GYLDEGYVRIKLKIEPGWDVEPVRAVRERFGDDVLLQVDANTAYTLGDAP
QLARLDPFGLLLIEQPLEEEDVLGHAELARRIQTPICLDESIVSARAAAD
AIKLGAVQIVNIKPGRVGGYLEARRVHDVCAAHGIPVWCGGMIETGLGRA
ANVALASLPNFTLPGDTSASDRFYKTDITEPFVLSGGHLPVPTGPGLGVA
PIPELLDEVTTAKVWIGS

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 1sjb Chain B Residue 1101

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1sjb Evolution of Enzymatic Activity in the Enolase Superfamily: Structural Studies of the Promiscuous o-Succinylbenzoate Synthase from Amycolatopsis
• Resolution: 2.2 Å
• Binding residue (original residue number in PDB): D189 E214 D239
• Binding residue (residue number reindexed from 1): D189 E214 D239
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): F19 S135 K161 K163 D189 N191 E214 D239 E240 S241 K263 G290 G291 M292 G315 D316 T317
• Catalytic site (residue number reindexed from 1): F19 S135 K161 K163 D189 N191 E214 D239 E240 S241 K263 G290 G291 M292 G315 D316 T317
• Enzyme Commision number: 4.2.1.113: o-succinylbenzoate synthase.
  5.1.1.-

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0016829 lyase activity
• GO:0016853 isomerase activity
• GO:0043748 O-succinylbenzoate synthase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0009234 menaquinone biosynthetic process

External links

• PDB: RCSB:1sjb, PDBe:1sjb, PDBj:1sjb
• PDBsum: 1sjb
• PubMed: 15134446
• UniProt: Q44244|NSAR_AMYSP N-succinylamino acid racemase (Gene Name=Aaar)