Structure of PDB 6jeq Chain A

Receptor sequence

>6jeqA (length=651) Species: 343517 (Paenibacillus barengoltzii)

QKEFHGTIDYGDVTVTGGISVFDAKFDELYVYDGDDLGAVYAPEETRFRL
WAPTASEAFVVLYETEDGMPVKELPMKRDVQGTWTLTVAEDCGGLFYTYR
VKVGEQWNEAVDPYAKAVGVNGTKTAILDLRSTNPEGWENDQKPPLASPT
DAVIYELHVRDLSIHPQSGIREKGKFLGLTEEGTRGPNGIPTGLDHITGL
GVTHVQLLPIYDYSQESVDESRLDEPHYNWGYDPQNYNVPEGSYSTDPHN
PAARILELKRLIQKLHARGLRVIMDVVYNHVYDGYLIHFTKLVPGYYLRY
KADRTFSDGTFCGNECASERPIMRKYIIESILHWVREYHIDGFRFDLMGM
IDIETMNEIRRRLDEIDPTILTIGEGWMMETVLPKELRANQDNAEKLPGI
GMFNDGMRDAVKGDIFIFDRKGFISGGDGFEDGVKRGVAGGINYGGQLRQ
FAVEPVQSVNYVECHDNHTLWDKIELSTPGASDEERRAMHRLASAIVLTS
QGIPFLHAGQEFMRTKGGVENSYKSPIEVNWLDWERCAAHQDDVSYMRSL
IALRKAHPAFRLKTADEIRAHLRFEAAPPHTVAFTLRDHAGGDPDRHLYV
LYNANPGALSLELPALGPWEVRFGGEHVLALEAGARLEVRGVGVVVLAVP
R

3D structure

• PDB: 6jeq Structural basis of carbohydrate binding in domain C of a type I pullulanase from Paenibacillus barengoltzii.
• Chain: A
• Resolution: 1.802 Å

Enzymatic activity

• Enzyme Commision number: 3.2.1.41: pullulanase.

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	W381 D409 R412 F420	W377 D405 R408 F416
BS02	GLC	A	R495 D546 S549	R491 D542 S545
BS03	GLC	A	S553 F627 G628 E630	S549 F623 G624 E626
BS04	GLC	A	R626 F627 G629	R622 F623 G625
BS05	CA	A	D216 Y217 E224 E245	D212 Y213 E220 E241

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0016798 hydrolase activity, acting on glycosyl bonds
• GO:0046872 metal ion binding
• GO:0051060 pullulanase activity

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:6jeq, PDBe:6jeq, PDBj:6jeq
• PDBsum: 6jeq
• PubMed: 32355041
• UniProt: A0A0C5GWS2