Structure of PDB 1qho Chain A

Receptor sequence

>1qhoA (length=686) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]

SSSASVKGDVIYQIIIDRFYDGDTTNNNPAKSYGLYDPTKSKWKMYWGGD
LEGVRQKLPYLKQLGVTTIWLSPVLDNLDTLAGTDNTGYHGYWTRDFKQI
EEHFGNWTTFDTLVNDAHQNGIKVIVDFVPNHSTPFKANDSTFAEGGALY
NNGTYMGNYFDDATKGYFHHNGDISNWDDRYEAQWKNFTDPAGFSLADLS
QENGTIAQYLTDAAVQLVAHGADGLRIDAVKHFNSGFSKSLADKLYQKKD
IFLVGEWYGDDPGTANHLEKVRYANNSGVNVLDFDLNTVIRNVFGTFTQT
MYDLNNMVNQTGNEYKYKENLITFIDNHDMSRFLSVNSNKANLHQALAFI
LTSRGTPSIYYGTEQYMAGGNDPYNRGMMPAFDTTTTAFKEVSTLAGLRR
NNAAIQYGTTTQRWINNDVYIYERKFFNDVVLVAINRNTQSSYSISGLQT
ALPNGSYADYLSGLLGGNGISVSNGSVASFTLAPGAVSVWQYSTSASAPQ
IGSVAPNMGIPGNVVTIDGKGFGTTQGTVTFGGVTATVKSWTSNRIEVYV
PNMAAGLTDVKVTAGGVSSNLYSYNILSGTQTSVVFTVKSAPPTNLGDKI
YLTGNIPELGNWSTDTSGAVNNAQGPLLAPNYPDWFYVFSVPAGKTIQFK
FFIKRADGTIQWENGSNHVATTPTGATGNITVTWQN

3D structure

PDB

1qho X-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution.

Chain

Resolution

1.7 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	D127 R226 D228 E256 H328 D329
Catalytic site (residue number reindexed from 1)	D127 R226 D228 E256 H328 D329
Enzyme Commision number	3.2.1.133: glucan 1,4-alpha-maltohydrolase.

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	K650 W662	K650 W662
BS02	GLC	A	W612 N667	W612 N667
BS03	GLC	A	W414 I415	W414 I415
BS04	GLC	A	Q412 R413 G447	Q412 R413 G447
BS05	BGC	A	Y258 G259 D261	Y258 G259 D261
BS06	GLC	A	K231 Y258	K231 Y258
BS07	AGL	A	A229 H232 E256 D329	A229 H232 E256 D329
BS08	GLC	A	Y92 H132 D228 E256 H328 D329	Y92 H132 D228 E256 H328 D329
BS09	GLC	A	Y92 W93 D190 D372 R376	Y92 W93 D190 D372 R376
BS10	GLC	A	T189 D190 P191 D372	T189 D190 P191 D372
BS11	CA	A	D76 N77 D79 E101 E102	D76 N77 D79 E101 E102
BS12	CA	A	N131 Q184 D198 H232	N131 Q184 D198 H232
BS13	CA	A	D21 D23 N26 N27 G48 D50	D21 D23 N26 N27 G48 D50

Gene Ontology

	Molecular Function
GO:0003824	catalytic activity
GO:0004556	alpha-amylase activity
GO:0030246	carbohydrate binding
GO:0043169	cation binding
GO:2001070	starch binding

	Biological Process
GO:0005975	carbohydrate metabolic process

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:1qho, PDBe:1qho, PDBj:1qho
PDBsum	1qho
PubMed	10387084
UniProt	P19531\|AMYM_GEOSE Maltogenic alpha-amylase (Gene Name=amyM)

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