Structure of PDB 5fjo Chain B

Receptor sequence

>5fjoB (length=368) Species: 37632 (Amycolatopsis sp.)

MKLSGVELRRVQMPLVAPFRTSFGTQSVRELLLLRAVTPAGEGWGECVTM
AGPLYSSEYNDGAEHVLRHYLIPALLAAEDITAAKVTPLLAKFKGHRMAK
GALEMAVLDAELRAHERSFAAELGSVRDSVPCGVSVGIMDTIPQLLDVVG
GYLDEGYVRIKLKIEPGWDVEPVRAVRERFGDDVLLQVDANTAYTLGDAP
QLARLDPFGLLLIEQPLEEEDVLGHAELARRIQTPICLDESIVSARAAAD
AIKLGAVQIVNIKPGRVGGYLEARRVHDVCAAHGIPVWCGDMIETGLGRA
ANVALASLPNFTLPGDTSASDRYYKTDITEPFVLSGGHLPVPTGPGLGVA
PIPELLDEVTTAKVWIGS

3D structure

• PDB: 5fjo Structure of N-Acylamino Acid Racemase Mutants in Complex with Substrates
• Chain: B
• Resolution: 2.08 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): F19 S135 K161 K163 D189 N191 E214 D239 E240 S241 K263 G290 D291 M292 G315 D316 T317
• Catalytic site (residue number reindexed from 1): F19 S135 K161 K163 D189 N191 E214 D239 E240 S241 K263 G290 D291 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	NPQ	B	F19 Q26 R29 M50 S135 K161 K163 N191 K263 D291 I293	F19 Q26 R29 M50 S135 K161 K163 N191 K263 D291 I293
BS02	MG	B	D189 E214 D239	D189 E214 D239

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:5fjo, PDBe:5fjo, PDBj:5fjo
• PDBsum: 5fjo
• UniProt: Q44244|NSAR_AMYSP N-succinylamino acid racemase (Gene Name=Aaar)