Structure of PDB 1itc Chain A

Receptor sequence

>1itcA (length=516) Species: 1396 (Bacillus cereus) [Search protein sequence]

AVNGKGMNPDYKAYLMAPLKKIPEVTNWETFENDLRWAKQNGFYAITVDF
WWGDMEKNGDQQFDFSYAQRFAQSVKNAGMKMIPIISTHQCGGNVGDDCN
VPIPSWVWNQKSDDSLYFKSETGTVNKETLNPLASDVIRKEYGELYTAFA
AAMKPYKDVIAKIYLSGGPAGALRYPSYTTSDGTGYPSRGKFQAYTEFAK
SKFRLWVLNKYGSLNEVNKAWGTKLISELAILPPSDGEQFLMNGYLSMYG
KDYLEWYQGILENHTKLIGELAHNAFDTTFQVPIGAKIAGVHWQYNNPTI
PHGAEKPAGYNDYSHLLDAFKSAKLDVTFTCLEMTDKGSYPEYSMPKTLV
QNIATLANEKGIVLNGENALSIGNEEEYKRVAEMAFNYNFAGFTLLRYQD
VMYNNSLMGKFKDLLGVTPVMQTIVVKNVPTTIGDTVYITGNRAELGSWD
TKQYPIQLYYDSHSNDWRGNVVLPAERNIEFKAFIKSKDGTVKSWQTIQQ
SWNPVPLKTTSHTSSW

3D structure

PDB

1itc Crystal Structure of a Catalytic Site Mutant of beta-Amylase from Bacillus cereus var. mycoides Cocrystallized with Maltopentaose

Chain

Resolution

2.1 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Catalytic site (original residue number in PDB)	D97 A172 T330 E367 L370
Catalytic site (residue number reindexed from 1)	D97 A172 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)
BS01	GLC	A	V95 L370	V95 L370
BS02	GLC	A	Y186 H292	Y186 H292
BS03	GLC	A	R174 Y178 G290 T330	R174 Y178 G290 T330
BS04	GLC	A	V95 K287 E367 A369	V95 K287 E367 A369
BS05	GLC	A	D49 H89 D97 R397	D49 H89 D97 R397
BS06	GLC	A	Q239 N243	Q239 N243
BS07	GLC	A	G244 Y249	G244 Y249
BS08	GLC	A	A230 I231 L232 S235 Y249	A230 I231 L232 S235 Y249
BS09	GLC	A	K482 W495	K482 W495
BS10	GLC	A	W449 Q499	W449 Q499
BS11	GLC	A	S188 R189 P341 Y343	S188 R189 P341 Y343
BS12	GLC	A	E238 N297 T299	E238 N297 T299
BS13	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

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:1itc, PDBe:1itc, PDBj:1itc
PDBsum	1itc
PubMed	12741813
UniProt	P36924\|AMYB_BACCE Beta-amylase (Gene Name=spoII)

[Back to BioLiP]