Structure of PDB 1j0z Chain C

Receptor sequence

>1j0zC (length=516) Species: 1396 (Bacillus cereus)

AVNGKGMNPDYKAYLMAPLKKIPEVTNWETFENDLRWAKQNGFYAITVDF
WWGDMEKNGDQQFDFSYAQRFAQSVKNAGMKMIPIISTHQCGGNVGDDCN
VPIPSWVWNQKSDDSLYFKSETGTVNKETLNPLASDVIRKEYGELYTAFA
AAMKPYKDVIAKIYLSGGPAGELRYPSYTTSDGTGYPSRGKFQAYTEFAK
SKFRLWVLNKYGSLNEVNKAWGTKLISELAILPPSDGEQFLMNGYLSMYG
KDYLEWYQGILENHTKLIGELAHNAFDTTFQVPIGAKIAGVHWQYNNPTI
PHGAEKPAGYNDYSHLLDAFKSAKLDVTFTCLEMTDKGSYPEYSMPKTLV
QNIATLANEKGIVLNGENALSIGNEEEYKRVAEMAFNYNFAGFTLLRYQD
VMYNNSLMGKFKDLLGVTPVMQTIVVKNVPTTIGDTVYITGNRAELGSWD
TKQYPIQLYYDSHSNDWRGNVVLPAERNIEFKAFIKSKDGTVKSWQTIQQ
SWNPVPLKTTSHTSSW

3D structure

• PDB: 1j0z Crystal Structures of beta-Amylase from Bacillus cereus var. mycoides in Complexes with Substrate Analogs and Affinity-Labeling Reagents
• Chain: C
• Resolution: 2.2 Å

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	GLC	C	E172 K287 T330 E367 A369 L396	E172 K287 T330 E367 A369 L396
BS02	GLC	C	M16 D49 H89 D97 A170 R397	M16 D49 H89 D97 A170 R397
BS03	BGC	C	P234 Q239 F240 G244 Y249	P234 Q239 F240 G244 Y249
BS04	GLC	C	W221 A230 I231 L232 S235 Y249	W221 A230 I231 L232 S235 Y249
BS05	CA	C	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

External links

• PDB: RCSB:1j0z, PDBe:1j0z, PDBj:1j0z
• PDBsum: 1j0z
• PubMed: 12761294
• UniProt: P36924|AMYB_BACCE Beta-amylase (Gene Name=spoII)