Structure of PDB 3k8l Chain A

Receptor sequence

>3k8lA (length=649) Species: 818 (Bacteroides thetaiotaomicron) [Search protein sequence]

WTALTASPDTWDETKRADISYQLLLYSFADSDGDGYGDLNGVTQKLDYLN
QLGVKALWLSPIHPCMSYHGYDVTDYTKVNPQLGTESDFDRLVTEAHNRG
IKIYLDYVMNHTGTAHPWFTEASSSSESPYRNYYSFSEDPKTDIAAGKIA
MITQEGAAGYNAAEWFQVSDETAAVKGLLKFTLDWSNAPSPILVVSTGTK
ADEDNPDTGTDNAKYLYYGEDICKKFYDKGNNIYELTVDFESTWGLLIRT
SNASFWPSGTKYGASSSSEKLALNKDFKLTNAGNPANIMFDSQQITYFHS
HFCTDWFADLNYGPVDQAGESPAYQAIADAAKGWIARGVDGLRLDAVKHI
YHSETSEENPRFLKMFYEDMNAYYKQKGHTDDFYMIGEVLSEYDKVAPYY
KGLPALFEFSFWYRLEWGINNSTGCYFAKDILSYQQKYANYRSDYIEATK
LSNHNEDRTSSKLGKSADKCKLAAAVLLTSAGHPYIYYGEELGLYGTKDN
GDEYVRSPMLWGDSYTTNYTDKTDATVSKNVKTVADQQADTHSLLNIYFS
LTRLRNTYPALAEGNMTKHSVYNESQEKDYKPIAAWYMTKDNEKLLVIHN
FGGTAMQLPLTDKIEKVLFVNGETQQNTDSDSYTLKLGGYASVVFKLGN

3D structure

PDB

3k8l SusG: A Unique Cell-Membrane-Associated alpha-Amylase from a Prominent Human Gut Symbiont Targets Complex Starch Molecules.

Chain

Resolution

2.3 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	D149 R386 D388 E431 H497 N498
Catalytic site (residue number reindexed from 1)	D106 R343 D345 E388 H454 N455
Enzyme Commision number	3.2.1.1: alpha-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	K391 L433	K348 L390
BS02	GLC	A	F345 A389 H392 E431	F302 A346 H349 E388
BS03	GLC	A	Y114 H154 F345 D388 E431 H497 N498	Y71 H111 F302 D345 E388 H454 N455
BS04	GLC	A	H112 Y114 F350 D545 R549	H69 Y71 F307 D502 R506
BS05	GLC	A	K541 D542 D545	K498 D499 D502
BS06	GLC	A	W299 K304	W256 K261
BS07	GLC	A	Y260 W287 N330	Y217 W244 N287
BS08	GLC	A	E263 W287	E220 W244
BS09	GLC	A	E435 D437	E392 D394
BS10	GLC	A	R457 W460	R414 W417
BS11	GLC	A	W460 D473	W417 D430
BS12	GLC	A	Y469 K472	Y426 K429
BS13	CA	A	D73 D75 D77 Y79 D81	D30 D32 D34 Y36 D38
BS14	CA	A	N153 D352 H392 I393	N110 D309 H349 I350

Gene Ontology

	Molecular Function
GO:0000287	magnesium ion binding
GO:0004556	alpha-amylase activity
GO:0005509	calcium ion binding
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:0005975	carbohydrate metabolic process
GO:0005983	starch catabolic process
GO:0009313	oligosaccharide catabolic process

	Cellular Component
GO:0009279	cell outer membrane
GO:0019867	outer membrane

View graph for
Molecular Function

View graph for
Biological Process

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Cellular Component

External links

PDB	RCSB:3k8l, PDBe:3k8l, PDBj:3k8l
PDBsum	3k8l
PubMed	20159465
UniProt	Q8A1G3\|SUSG_BACTN Alpha-amylase SusG (Gene Name=susG)

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