Structure of PDB 5fjp Chain A

Receptor sequence
>5fjpA (length=368) Species: 37632 (Amycolatopsis sp.) [Search protein sequence]
MKLSGVELRRVQMPLVAPFRTSFGTQSVRELLLLRAVTPAGEGWGECVTM
AGPLYSSEYNDGAEHVLRHYLIPALLAAEDITAAKVTPLLAKFKGHRMAK
GALEMAVLDAELRAHERSFAAELGSVRDSVPCGVSVGIMDTIPQLLDVVG
GYLDEGYVRIKLKIEPGWDVEPVRAVRERFGDDVLLQVDANTAYTLGDAP
QLARLDPFGLLLIEQPLEEEDVLGHAELARRIQTPICLDESIVSARAAAD
AIKLGAVQIVNIKPGRVGGYLEARRVHDVCAAHGIPVWCGDMGETGLGRA
ANVALASLPNFTLPGDTSASDRYYKTDITEPFVLSGGHLPVPTGPGLGVA
PIPELLDEVTTAKVWIGS
3D structure
PDB5fjp Structure of N-Acylamino Acid Racemase Mutants in Complex with Substrates
ChainA
Resolution2.58 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 A F19 Q26 M50 S135 K161 K163 K263 D291 Y323 F19 Q26 M50 S135 K161 K163 K263 D291 Y323
BS02 MG A 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

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Molecular Function
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Biological Process
External links
PDB RCSB:5fjp, PDBe:5fjp, PDBj:5fjp
PDBsum5fjp
PubMed
UniProtQ44244|NSAR_AMYSP N-succinylamino acid racemase (Gene Name=Aaar)

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