Structure of PDB 3p0w Chain A

Receptor sequence
>3p0wA (length=424) Species: 402626 (Ralstonia pickettii 12J) [Search protein sequence]
HTPRVTEMQVIPVAGRDSMLLNLCGAHAPFFTRNLVILKDNAGRTGVGEV
PGGEGIRQALERVIPLVVGQSIGRTNGVLSSIRRALARMDNVITAVEAAL
LDLLGQFLEVPVAELLGAGQQRDSAPMLAYLFYVGDRRKTDLPYLEGANG
ADDWLRLRHEAAMTPAAIARLAEAATERYGFADFKLKGGVMPGAEEMEAI
AAIKARFPHARVTLDPNGAWSLNEAIALCKGQGHLVAYAEDPCGPEAGYS
GREVMAEFKRATGIPTATNMIATDWRQMGHAVQLHAVDIPLADPHFWTMQ
GSVRVAQLCDEWGLTWGSHSNNHFDVSLAMFTHVAAAAPGNITAIDTHWI
WQEAQERLTREPLRIQGGHVAVPERPGLGIEIDMDRVMAAHALYKTLGPG
ARDDAMAMQYLVPGWTYDPKRPSL
3D structure
PDB3p0w Crystal structure of D-Glucarate dehydratase from Ralstonia solanacearum complexed with Mg and D-glucarate
ChainA
Resolution1.71 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K221 K223 D251 N253 E276 N305 D329 H355 N357
Catalytic site (residue number reindexed from 1) K185 K187 D215 N217 E240 N269 D293 H319 N321
Enzyme Commision number 4.2.1.40: glucarate dehydratase.
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 D251 E276 N305 D215 E240 N269
BS02 GKR A N27 H32 Y166 K223 D251 N253 N305 N357 H384 R438 N22 H27 Y130 K187 D215 N217 N269 N321 H348 R402
Gene Ontology
Molecular Function
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:3p0w, PDBe:3p0w, PDBj:3p0w
PDBsum3p0w
PubMed
UniProtB2UIZ1

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