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BioLiP

Structure of PDB 1sja Chain D

Receptor sequence
>1sjaD (length=368) Species: 37632 (Amycolatopsis sp.) [Search protein sequence]
MKLSGVELRRVQMPLVAPFRTSFGTQSVRELLLLRAVTPAGEGWGECVTM
AGPLYSSEYNDGAEHVLRHYLIPALLAAEDITAAKVTPLLAKFKGHRMAK
GALEMAVLDAELRAHERSFAAELGSVRDSVPCGVSVGIMDTIPQLLDVVG
GYLDEGYVRIKLKIEPGWDVEPVRAVRERFGDDVLLQVDANTAYTLGDAP
QLARLDPFGLLLIEQPLEEEDVLGHAELARRIQTPICLDESIVSARAAAD
AIKLGAVQIVNIKPGRVGGYLEARRVHDVCAAHGIPVWCGGMIETGLGRA
ANVALASLPNFTLPGDTSASDRFYKTDITEPFVLSGGHLPVPTGPGLGVA
PIPELLDEVTTAKVWIGS
3D structure
PDB1sja Evolution of Enzymatic Activity in the Enolase Superfamily: Structural Studies of the Promiscuous o-Succinylbenzoate Synthase from Amycolatopsis
ChainD
Resolution2.3 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 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 AME D F19 S135 K161 K163 D189 N191 E214 D239 K263 G291 F19 S135 K161 K163 D189 N191 E214 D239 K263 G291
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:1sja, PDBe:1sja, PDBj:1sja
PDBsum1sja
PubMed15134446
UniProtQ44244|NSAR_AMYSP N-succinylamino acid racemase (Gene Name=Aaar)

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