Structure of PDB 1j0z Chain A

Receptor sequence
>1j0zA (length=516) Species: 1396 (Bacillus cereus) [Search protein sequence]
AVNGKGMNPDYKAYLMAPLKKIPEVTNWETFENDLRWAKQNGFYAITVDF
WWGDMEKNGDQQFDFSYAQRFAQSVKNAGMKMIPIISTHQCGGNVGDDCN
VPIPSWVWNQKSDDSLYFKSETGTVNKETLNPLASDVIRKEYGELYTAFA
AAMKPYKDVIAKIYLSGGPAGELRYPSYTTSDGTGYPSRGKFQAYTEFAK
SKFRLWVLNKYGSLNEVNKAWGTKLISELAILPPSDGEQFLMNGYLSMYG
KDYLEWYQGILENHTKLIGELAHNAFDTTFQVPIGAKIAGVHWQYNNPTI
PHGAEKPAGYNDYSHLLDAFKSAKLDVTFTCLEMTDKGSYPEYSMPKTLV
QNIATLANEKGIVLNGENALSIGNEEEYKRVAEMAFNYNFAGFTLLRYQD
VMYNNSLMGKFKDLLGVTPVMQTIVVKNVPTTIGDTVYITGNRAELGSWD
TKQYPIQLYYDSHSNDWRGNVVLPAERNIEFKAFIKSKDGTVKSWQTIQQ
SWNPVPLKTTSHTSSW
3D structure
PDB1j0z Crystal Structures of beta-Amylase from Bacillus cereus var. mycoides in Complexes with Substrate Analogs and Affinity-Labeling Reagents
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D97 E172 T330 E367 L370
Catalytic site (residue number reindexed from 1) D97 E172 T330 E367 L370
Enzyme Commision number 3.2.1.2: beta-amylase.
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 E172 T330 E367 A369 E172 T330 E367 A369
BS02 GLC A M16 D49 H89 D97 R397 M16 D49 H89 D97 R397
BS03 BGC A Q239 F240 G244 Y249 Q239 F240 G244 Y249
BS04 GLC A A230 I231 L232 S235 Y249 A230 I231 L232 S235 Y249
BS05 CA A E56 D60 Q61 E141 E144 E56 D60 Q61 E141 E144
Gene Ontology
Molecular Function
GO:0016161 beta-amylase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
GO:2001070 starch binding
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005976 polysaccharide metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1j0z, PDBe:1j0z, PDBj:1j0z
PDBsum1j0z
PubMed12761294
UniProtP36924|AMYB_BACCE Beta-amylase (Gene Name=spoII)

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