Structure of PDB 1byh Chain A

Receptor sequence
>1byhA (length=214) Species: 32630 (synthetic construct) [Search protein sequence]
QTGGSFFEPFNSYNSGTWEKADGYSNGGVFNCTWRANNVNFTNDGKLKLG
LTSSAYNKFDCAEYRSTNIYGYGLYEVSMKPAKNTGIVSSFFTYTGPAHG
TQWDEIDIEFLGKDTTKVQFNYYTNGVGGHEKVISLGFDASKGFHTYAFD
WQPGYIKWYVDGVLKHTATANIPSTPGKIMMNLWNGTGVDDWLGSYNGAN
PLYAEYDWVKYTSN
3D structure
PDB1byh Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E105 D107 E109
Catalytic site (residue number reindexed from 1) E105 D107 E109
Enzyme Commision number 3.2.1.73: licheninase.
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 N26 E63 N26 E63
BS02 BGC A Y24 N26 Y94 H99 Y24 N26 Y94 H99
BS03 CA A P9 F10 G45 D207 P9 F10 G45 D207
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0042972 licheninase activity
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1byh, PDBe:1byh, PDBj:1byh
PDBsum1byh
PubMed8099449
UniProtP23904|GUB_PAEMA Beta-glucanase

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