Structure of PDB 1sjb Chain D

Receptor sequence

>1sjbD (length=368) Species: 37632 (Amycolatopsis sp.)

MKLSGVELRRVQMPLVAPFRTSFGTQSVRELLLLRAVTPAGEGWGECVTM
AGPLYSSEYNDGAEHVLRHYLIPALLAAEDITAAKVTPLLAKFKGHRMAK
GALEMAVLDAELRAHERSFAAELGSVRDSVPCGVSVGIMDTIPQLLDVVG
GYLDEGYVRIKLKIEPGWDVEPVRAVRERFGDDVLLQVDANTAYTLGDAP
QLARLDPFGLLLIEQPLEEEDVLGHAELARRIQTPICLDESIVSARAAAD
AIKLGAVQIVNIKPGRVGGYLEARRVHDVCAAHGIPVWCGGMIETGLGRA
ANVALASLPNFTLPGDTSASDRFYKTDITEPFVLSGGHLPVPTGPGLGVA
PIPELLDEVTTAKVWIGS

3D structure

• PDB: 1sjb Evolution of Enzymatic Activity in the Enolase Superfamily: Structural Studies of the Promiscuous o-Succinylbenzoate Synthase from Amycolatopsis
• Chain: D
• Resolution: 2.2 Å

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.-

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	MG	D	D189 E214 D239	D189 E214 D239
BS02	OSB	D	F19 F23 Y55 S135 K161 K163 D189 K263 G291 M292 I293 F323	F19 F23 Y55 S135 K161 K163 D189 K263 G291 M292 I293 F323

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)