Structure of PDB 2o0v Chain A

Receptor sequence
>2o0vA (length=399) Species: 1423 (Bacillus subtilis) [Search protein sequence]
ADLGHQTLGSNDGWGAYSTGTTGGSKASSSNVYTVSNRNQLVSALGKETN
TTPKIIYIKGTIDMNVDDNLKPLGLNDYKDPEYDLDKYLKAYDPSTWGKK
EPSGTQEEARARSQKNQKARVMVDIPANTTIVGSGTNAKVVGGNFQIKSD
NVIIRNIEFQDAYDYFPQWDPTDGSSGNWNSQYDNITINGGTHIWIDHCT
FNDGSRPDSTSPKYYGRKYQHHDGQTDASNGANYITMSYNYYHDHDKSSI
FGSSDSKTSDDGKLKITLHHNRYKNIVQAAPRVRFGQVHVYNNYYEGSTS
SSSYPFSYAWGIGKSSKIYAQNNVIDVPGLSAAKTISVFSGGTALYDSGT
LLNGTQINASAANGLSSSVGWTPSLHGSIDASANVKSNVINQAGAGKLN
3D structure
PDB2o0v Structural insights into substrate specificity and the anti beta-elimination mechanism of pectate lyase.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D184 D223 D227 A279
Catalytic site (residue number reindexed from 1) D184 D223 D227 A279
Enzyme Commision number 4.2.2.2: pectate lyase.
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 ADA A D173 R282 F339 D173 R282 F339
BS02 ADA A K247 I250 R284 K247 I250 R284
BS03 ADA A Q182 S253 K257 Q182 S253 K257
BS04 CA A D184 D223 D227 D184 D223 D227
BS05 CA A D173 N180 D173 N180
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:2o0v, PDBe:2o0v, PDBj:2o0v
PDBsum2o0v
PubMed20000851
UniProtP39116|PLY_BACSU Pectate lyase (Gene Name=pel)

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