Structure of PDB 2zad Chain A

Receptor sequence
>2zadA (length=344) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
SRIVNVKLSLKRYEYEKPFHITGSVSSESRNVEVEIVLESGVKGYGEASP
SFRVNGERVEALLAIENAVREMITGIDVRNYARIFEITDRLFGFPSLKAA
VQFATLDALSQELGTQVCYLLGGKRDEIETDKTVGIDTVENRVKEAKKIF
EEGFRVIKIKVGENLKEDIEAVEEIAKVTRGAKYIVDANMGYTQKEAVEF
ARAVYQKGIDIAVYEQPVRREDIEGLKFVRFHSPFPVAADESARTKFDVM
RLVKEEAVDYVNIKLMKSGISDALAIVEIAESSGLKLMIGCMGESSLGIN
QSVHFALGTGAFEFHDLDSHLMLKEEVFRGKFIQDGPRMRVKDQ
3D structure
PDB2zad Crystal Structure of Muconate Cycloisomerase from Thermotoga maritima MSB8
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F20 T134 K159 K161 D188 E216 D241 E242 S243 K265 G291 C292 M293 H316 D317 L318
Catalytic site (residue number reindexed from 1) F19 T133 K158 K160 D187 E215 D240 E241 S242 K264 G290 C291 M292 H315 D316 L317
Enzyme Commision number 5.1.1.20: L-Ala-D/L-Glu epimerase.
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 MN A D188 E216 D241 D187 E215 D240
Gene Ontology
Molecular Function
GO:0016853 isomerase activity
GO:0016854 racemase and epimerase activity
GO:0016855 racemase and epimerase activity, acting on amino acids and derivatives
GO:0046872 metal ion binding
GO:0103031 L-Ala-D/L-Glu epimerase activity
Biological Process
GO:0016998 cell wall macromolecule catabolic process
GO:0071555 cell wall organization

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Molecular Function
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Biological Process
External links
PDB RCSB:2zad, PDBe:2zad, PDBj:2zad
PDBsum2zad
PubMed
UniProtQ9WXM1|AEEP_THEMA L-Ala-D/L-Glu epimerase (Gene Name=TM_0006)

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