Structure of PDB 3p3b Chain A

Receptor sequence
>3p3bA (length=377) Species: 481743 (Paenibacillus sp. Y412MC10) [Search protein sequence]
LNITGIQSDWKVEKIEFAKLTGERARSAGANGRIGVHGKSCTVDIARITI
DGQTGYGSSIHMTPEWAEDVIGRRLLDLFDDRGRLREAYRLQLEYPVLDW
LGQRQGKPVYDLVSSLVVPCYDTSLYFDDLHLADERAAVALMQEEAMQGY
AKGQRHFKIKVGRGGRHMPLWEGTKRDIAIVRGISEVAGPAGKIMIDANN
AYNLNLTKEVLAALSDVNLYWLEEAFHEDEALYEDLKEWLGQRGQNVLIA
DGEGLASPHLIEWATRGRVDVLQYDIIWPGFTHWMELGEKLDAHGLRSAP
HCYGNAYGIYASGHLSAAVRNFEFVEYDDITIEGMDVSGYRIENGEIHVP
ATPGFGIVFDDELVTYLINRSGWSEGH
3D structure
PDB3p3b CRYSTAL STRUCTURE OF Galacturonate DEHYDRATASE FROM GEOBACILLUS SP. COMPLEXED WITH D-TARTRATE.
ChainA
Resolution1.651 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D207 E233 E263 D285 H311
Catalytic site (residue number reindexed from 1) D197 E223 E253 D275 H301
Enzyme Commision number ?
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 D207 E233 E263 D197 E223 E253
BS02 MG A E234 E238 D261 E224 E228 D251
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016836 hydro-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0016052 carbohydrate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3p3b, PDBe:3p3b, PDBj:3p3b
PDBsum3p3b
PubMed
UniProtD3EID5

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