Structure of PDB 2jeq Chain A

Receptor sequence
>2jeqA (length=359) Species: 1472 (Paenibacillus pabuli) [Search protein sequence]
QIVSEMGAGWNLGNQLEAAVNGTPNETAWGNPTVTPELIKKVKAAGFKSI
RIPVSYLNNIGSAPNYTINAAWLNRIQQVVDYAYNEGLYVIINIHGDGYN
SVQGGWLLVNGGNQTAIKEKYKKVWQQIATKFSNYNDRLIFESMNEVFDG
NYGNPNSAYYTNLNAYNQIFVDTVRQTGGNNNARWLLVPGWNTNIDYTVG
NYGFTLPTDNYRSSAIPSSQKRIMISAHYYSPWDFAGEENGNITQWGATS
TNPAKKSTWGQEDYLESQFKSMYDKFVTQGYPVVIGEFGSIDKTSYDSSN
NVYRAAYAKAVTAKAKKYKMVPVYWDNGHNGQHGFALFNRSNNTVTQQNI
INAIMQGMQ
3D structure
PDB2jeq Characterization and Three-Dimensional Structures of Two Distinct Bacterial Xyloglucanases from Families Gh5 and Gh12.
ChainA
Resolution1.94 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.151: xyloglucan-specific endo-beta-1,4-glucanase.
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 BGC A H131 Y135 E182 Y266 E323 W361 H95 Y99 E146 Y230 E287 W325
BS02 BGC A N50 W65 N363 N14 W29 N327
BS03 XYS A Y135 S137 Y99 S101
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2jeq, PDBe:2jeq, PDBj:2jeq
PDBsum2jeq
PubMed17376777
UniProtH9KVH3

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