Structure of PDB 1ven Chain A

Receptor sequence

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

AVNGKGMNPDYKAYLMAPLKKIPEVTNWETFENDLRWAKQNGFYAITVDF
WWGDMEKNGDQQFDFSYAQRFAQSVKNAGMKMIPIISTHQCGGNVGDDCN
VPIPSWVWNQKSDDSLYFKSETGTVNKETLNPLASDVIRKEYGELYTAFA
AAMKPYKDVIAKIELSGGPAGELRYPSYTTSDGTGYPSRGKFQAYTEFAK
SKFRLWVLNKYGSLNEVNKAWGTKLISELAILPPSDGEQFLMNGYLSMYG
KDYLEWYQGILENHTKLIGELAHNAFDTTFQVPIGAKIAGVHWQYNNPTI
PHGAEKPAGYNDYSHLLDAFKSAKLDVTFTCLEMTDKGSYPEYSMPKTLV
QNIATLANEKGIVLNGENALSIGNEEEYKRVAEMAFNYNFAGFTLLRYQD
VMYNNSLMGKFKDLLGVTPVMQTIVVKNVPTTIGDTVYITGNRAELGSWD
TKQYPIQLYYDSHSNDWRGNVVLPAERNIEFKAFIKSKDGTVKSWQTIQQ
SWNPVPLKTTSHTSSW

3D structure

• PDB: 1ven Engineering of the pH optimum of Bacillus cereus beta-amylase: conversion of the pH optimum from a bacterial type to a higher-plant type
• Chain: A
• Resolution: 2.02 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	A	M16 D49 H89 D97 R397	M16 D49 H89 D97 R397
BS02	GLC	A	V95 Y178 Y186	V95 Y178 Y186
BS03	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

External links

• PDB: RCSB:1ven, PDBe:1ven, PDBj:1ven
• PDBsum: 1ven
• PubMed: 15449941
• UniProt: P36924|AMYB_BACCE Beta-amylase (Gene Name=spoII)