Structure of PDB 5fjp Chain C

Receptor sequence

>5fjpC (length=367) Species: 37632 (Amycolatopsis sp.)

MKLSGVELRRVQMPLVAPFRTSFGTQSVRELLLLRAVTPAGEGWGECVTM
AGPLYSSEYNDGAEHVLRHYLIPALLAAEDITAAKVTPLLAKFKGHRMAK
GALEMAVLDAELRAHERSFAAELGSVRDSVPCGVSVGIMDTIPQLLDVVG
GYLDEGYVRIKLKIEPGWDVEPVRAVRERFGDDVLLQVDANTAYTLGDAP
QLARLDPFGLLLIEQPLEEEDVLGHAELARRIQTPICLDESIVSARAAAD
AIKLGAVQIVNIKPGRVGGYLEARRVHDVCAAHGIPVWCGDMGETGLGRA
ANVALASLPNFTLPGDTSASDRYYKTDITEPFVLSGGHLPVPTGPGLGVA
PIPELLDEVTTAKVWIG

3D structure

• PDB: 5fjp Structure of N-Acylamino Acid Racemase Mutants in Complex with Substrates
• Chain: C
• Resolution: 2.58 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	C	F19 Q26 R29 M50 S135 K161 K163 K263 D291 M292 Y323	F19 Q26 R29 M50 S135 K161 K163 K263 D291 M292 Y323
BS02	MG	C	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:5fjp, PDBe:5fjp, PDBj:5fjp
• PDBsum: 5fjp
• UniProt: Q44244|NSAR_AMYSP N-succinylamino acid racemase (Gene Name=Aaar)