Structure of PDB 1xs2 Chain A

Receptor sequence

>1xs2A (length=360) Species: 1299 (Deinococcus radiodurans)

RMFKIEAAEIVVARLPLKTHKVVPLLILHGEGVQGVAEGTMEARPMYREE
TIAGALDLLRGTFLPAILGQTFANPEAVSDALGSYRGNRMARAMVEMAAW
DLWARTLGVPLGTLLGGHKEQVEVGVSLGIQADEQATVDLVRRHVEQGYR
RIKLKIKPGWDVQPVRATREAFPDIRLTVDANSAYTLADAGRLRQLDEYD
LTYIEQPLAWDDLVDHAELARRIRTPLCLDESVASASDARKALALGAGGV
INLKVARVGGHAESRRVHDVAQSFGAPVWCGGMLESGIGRAHNIHLSTLS
NFRLPGDTSSASRYWERDLIQEPLEAVDGLMPVPQGPGTGVTLDREFLAT
VTEAQEEHRA

3D structure

• PDB: 1xs2 Structural basis for catalytic racemization and substrate specificity of an N-acylamino acid racemase homologue from Deinococcus radiodurans
• Chain: A
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): M56 R59 S142 K168 K170 R191 T193 D195 N197 E220 D245 E246 S247 K269 C295 G296 G297 M298 G321 D322 T323
• Catalytic site (residue number reindexed from 1): M41 R44 S127 K153 K155 R176 T178 D180 N182 E205 D230 E231 S232 K254 C280 G281 G282 M283 G306 D307 T308
• 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	A	K168 E220	K153 E205

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:1xs2, PDBe:1xs2, PDBj:1xs2
• PDBsum: 1xs2
• PubMed: 15313614
• UniProt: Q9RYA6|NSAR_DEIRA N-succinylamino acid racemase (Gene Name=DR_0044)