Structure of PDB 1u0a Chain D

Receptor sequence
>1u0aD (length=214) Species: 44252 (Paenibacillus macerans) [Search protein sequence]
QTGGSFFEPFNSYNSGTWEKADGYSNGGVFNCTWRANNVNFTNDGKLKLG
LTSSAYNKFDCAEYRSTNIYGYGLYEVSMKPAKNTGIVSSFFTYTGPAHG
TQWDQIDIQFLGKDTTKVQFNYYTNGVGGHEKVISLGFDASKGFHTYAFD
WQPGYIKWYVDGVLKHTATANIPSTPGKIMMNLWNGTGVDDWLGSYNGAN
PLYAEYDWVKYTSN
3D structure
PDB1u0a Structural Basis for the Substrate Specificity of a Bacillus 1,3-1,4-beta-Glucanase
ChainD
Resolution1.64 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q1005 D1007 Q1009
Catalytic site (residue number reindexed from 1) Q105 D107 Q109
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 D F930 S990 F992 Q1005 D1007 Q1009 N1082 W1084 F30 S90 F92 Q105 D107 Q109 N182 W184
BS02 BGC D N926 E963 Y994 N26 E63 Y94
BS03 BGC D Y924 R965 H999 Y24 R65 H99
BS04 ZN D H1045 D1061 H145 D161
BS05 CA D P909 G945 D1107 P9 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:1u0a, PDBe:1u0a, PDBj:1u0a
PDBsum1u0a
PubMed16483609
UniProtP23904|GUB_PAEMA Beta-glucanase

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