Structure of PDB 6jhh Chain A

Receptor sequence

>6jhhA (length=642) Species: 343517 (Paenibacillus barengoltzii)

YGDVTVTGGISVFDAKFDELYVYDGDDLGAVYAPEETRFRLWAPTASEAF
VVLYETEDGMPVKELPMKRDVQGTWTLTVAEDCGGLFYTYRVKVGEQWNE
AVDPYAKAVGVNGTKTAILDLRSTNPEGWENDQKPPLASPTDAVIYELHV
RDLSIHPQSGIREKGKFLGLTEEGTRGPNGIPTGLDHITGLGVTHVQLLP
IYDYSQESVDESRLDEPHYNWGYDPQNYNVPEGSYSTDPHNPAARILELK
RLIQKLHARGLRVIMDVVYNHVYDGYLIHFTKLVPGYYLRYKADRTFSDG
TFCGNECASERPIMRKYIIESILHWVREYHIDGFRFALMGMIDIETMNEI
RRRLDEIDPTILTIGEGWMMETVLPKELRANQDNAEKLPGIGMFNDGMRD
AVKGDIFIFDRKGFISGGDGFEDGVKRGVAGGINYGGQLRQFAVEPVQSV
NYVECHDNHTLWDKIELSTPGASDEERRAMHRLASAIVLTSQGIPFLHAG
QEFMRTKGGVENSYKSPIEVNWLDWERCAAHQDDVSYMRSLIALRKAHPA
FRLKTADEIRAHLRFEAAPPHTVAFTLRDHAGGDPDRHLYVLYNANPGAL
SLELPALGPWEVRFGGEHVLALEAGARLEVRGVGVVVLAVPR

3D structure

• PDB: 6jhh Crystal structure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose
• Chain: A
• Resolution: 2.025 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	W234 Y236 C316 R348 A350 E379 H469 D470	W221 Y223 C303 R335 A337 E366 H456 D457
BS02	GLC	A	Y236 D237 N525	Y223 D224 N512
BS03	GLC	A	F315 Y527	F302 Y514
BS04	GLC	A	W381 D409 R412 F420	W368 D396 R399 F407
BS05	GLC	A	F315 N471	F302 N458
BS06	GLC	A	R495 S549	R482 S536
BS07	GLC	A	S553 F627 G628 E630	S540 F614 G615 E617
BS08	CA	A	D216 Y217 E224 E245	D203 Y204 E211 E232

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:6jhh, PDBe:6jhh, PDBj:6jhh
• PDBsum: 6jhh
• UniProt: A0A0C5GWS2