Structure of PDB 1e4i Chain A

Receptor sequence
>1e4iA (length=447) Species: 1406 (Paenibacillus polymyxa) [Search protein sequence]
TIFQFPQDFMWGTATAAYQIEGAYQEDGRGLSIWDTFAHTPGKVFNGDNG
NVACDSYHRYEEDIRLMKELGIRTYRFSVSWPRIFPNGDGEVNQKGLDYY
HRVVDLLNDNGIEPFCTLYHWDLPQALQDAGGWGNRRTIQAFVQFAETMF
REFHGKIQHWLTFNEPWCIAFLSNMLGVHAPGLTNLQTAIDVGHHLLVAH
GLSVRRFRELGTSGQIGIAPNVSWAVPYSTSEEDKAACARTISLHSDWFL
QPIYQGSYPQFLVDWFAEQGATVPIQDGDMDIIGEPIDMIGINYYSMSVN
RFNPEAGFLQSEEINMGLPVTDIGWPVESRGLYEVLHYLQKYGNIDIYIT
ENGACINDEVVNGKVQDDRRISYMQQHLVQVHRTIHDGLHVKGYMAWSLL
DNFEWAEGYNMRFGMIHVDFRTQVRTPKQSYYWYRNVVSNNWLETRR
3D structure
PDB1e4i Structural Basis of Increased Resistance to Thermal Denaturation Induced by Single Amino Acid Substitution in the Sequence of Beta-Glucosidase a from Bacillus Polymyxa.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R77 H121 E166 C169 N294 Y296 E352
Catalytic site (residue number reindexed from 1) R76 H120 E165 C168 N293 Y295 E351
Enzyme Commision number 3.2.1.21: beta-glucosidase.
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 G2F A Q20 H121 N165 E166 Y296 E352 W398 E405 W406 Q19 H120 N164 E165 Y295 E351 W397 E404 W405
BS02 NFG A R137 Q141 V144 L203 R136 Q140 V143 L202
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0016052 carbohydrate catabolic process
GO:0030245 cellulose catabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1e4i, PDBe:1e4i, PDBj:1e4i
PDBsum1e4i
PubMed9849940
UniProtP22073|BGLA_PAEPO Beta-glucosidase A (Gene Name=bglA)

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