Structure of PDB 3qpe Chain D

Receptor sequence
>3qpeD (length=385) Species: 481743 (Paenibacillus sp. Y412MC10) [Search protein sequence]
LNITGIQSDWKVEKIEFAKLTGERARSAGANGRIGVHGKSCTVDIARITI
DGQTGYGSSIHMTPEWAEDVIGRRLLDLFDDRGRLREAYRLQLEYPVLDW
LGQRQGKPVYDLVSGAHLETGASLVVPCYDTSLYFDDLHLADERAAVALM
QEEAMQGYAKGQRHFKIKVGRGGRHMPLWEGTKRDIAIVRGISEVAGPAG
KIMIDANNAYNLNLTKEVLAALSDVNLYWLEEAFHEDEALYEDLKEWLGQ
RGQNVLIADGEGLASPHLIEWATRGRVDVLQYDIIWPGFTHWMELGEKLD
AHGLRSAPHCYGNAYGIYASGHLSAAVRNFEFVEYDDITIEGMDVSGYRI
ENGEIHVPATPGFGIVFDDELVTYLINRSGWSEGH
3D structure
PDB3qpe Crystal structure of Galacturonate Dehydratase from GEOBACILLUS SP. complexed with D-Galacturonate and 5-keto-4-deoxy-D-Galacturonate
ChainD
Resolution1.796 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) D205 E231 E261 D283 H309
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 D D207 E233 E263 D205 E231 E261
BS02 MG D E234 E238 D261 E232 E236 D259
BS03 D54 D N33 H39 Y136 K168 K170 D207 E263 H311 E336 N31 H37 Y134 K166 K168 D205 E261 H309 E334
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:3qpe, PDBe:3qpe, PDBj:3qpe
PDBsum3qpe
PubMed
UniProtD3EID5

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