Structure of PDB 3krg Chain A Binding Site BS01

Receptor Information
>3krg Chain A (length=399) Species: 1423 (Bacillus subtilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ADLGHQTLGSNDGWGAYSTGTTGGSKASSSNVYTVSNRNQLVSALGKETN
TTPKIIYIKGTIDMNVDDNLKPLGLNDYKDPEYDLDKYLKAYDPSTWGKK
EPSGTQEEARARSQKNQKARVMVDIPANTTIVGSGTNAKVVGGNFQIKSD
NVIIRNIEFQDAYDYFPQWDPTAGSSGNWASQYDNITINGGTHIWIDHCT
FNDGSRPDSTSPKYYGRKYQHHDGQTDASNGANYITMSYNYYHDHDASSI
FGSSDSKTSDDGKLKITLHHNRYKNIVQRAPRVRFGQVHVYNNYYEGSTS
SSSYPFSYAWGIGKSSKIYAQNNVIDVPGLSAAKTISVFSGGTALYDSGT
LLNGTQINASAANGLSSSVGWTPSLHGSIDASANVKSNVINQAGAGKLN
Ligand information
Ligand IDADA
InChIInChI=1S/C6H10O7/c7-1-2(8)4(5(10)11)13-6(12)3(1)9/h1-4,6-9,12H,(H,10,11)/t1-,2+,3+,4-,6-/m0/s1
InChIKeyAEMOLEFTQBMNLQ-BKBMJHBISA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1(C(C(OC(C1O)O)C(=O)O)O)O
CACTVS 3.341O[CH]1O[CH]([CH](O)[CH](O)[CH]1O)C(O)=O
CACTVS 3.341O[C@H]1O[C@@H]([C@H](O)[C@H](O)[C@H]1O)C(O)=O
ACDLabs 10.04O=C(O)C1OC(O)C(O)C(O)C1O
OpenEye OEToolkits 1.5.0[C@@H]1([C@H]([C@H](O[C@@H]([C@@H]1O)O)C(=O)O)O)O
FormulaC6 H10 O7
Namealpha-D-galactopyranuronic acid;
alpha-D-galacturonic acid;
D-galacturonic acid;
galacturonic acid;
ALPHA D-GALACTURONIC ACID
ChEMBL
DrugBankDB03511
ZINCZINC000004228259
PDB chain3krg Chain B Residue 1 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3krg Structural insights into substrate specificity and the anti beta-elimination mechanism of pectate lyase
Resolution1.9 Å
Binding residue
(original residue number in PDB)		R279 R282 F339
Binding residue
(residue number reindexed from 1)		R279 R282 F339
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) Q182 D184 D223 D227 R279
Catalytic site (residue number reindexed from 1) Q182 D184 D223 D227 R279
Enzyme Commision number 4.2.2.2: pectate lyase.
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0030570 pectate lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0045490 pectin catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3krg, PDBe:3krg, PDBj:3krg
PDBsum3krg
PubMed20000851
UniProtP39116|PLY_BACSU Pectate lyase (Gene Name=pel)

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