Structure of PDB 6jhi Chain A

Receptor sequence
>6jhiA (length=646) Species: 343517 (Paenibacillus barengoltzii) [Search protein sequence]
HGTIDYGDVTVTGGISVFDAKFDELYVYDGDDLGAVYAPEETRFRLWAPT
ASEAFVVLYETEDGMPVKELPMKRDVQGTWTLTVAEDCGGLFYTYRVKVG
EQWNEAVDPYAKAVGVNGTKTAILDLRSTNPEGWENDQKPPLASPTDAVI
YELHVRDLSIHPQSGIREKGKFLGLTEEGTRGPNGIPTGLDHITGLGVTH
VQLLPIYDYSQESVDESRLDEPHYNWGYDPQNYNVPEGSYSTDPHNPAAR
ILELKRLIQKLHARGLRVIMDVVYNHVYDGYLIHFTKLVPGYYLRYKADR
TFSDGTFCGNECASERPIMRKYIIESILHWVREYHIDGFRFDLMGMIDIE
TMNEIRRRLDEIDPTILTIGEGWMMETVLPKELRANQDNAEKLPGIGMFN
DGMRDAVKGDIFIFDRKGFISGGDGFEDGVKRGVAGGINYGGQLRQFAVE
PVQSVNYVECHANHTLWDKIELSTPGASDEERRAMHRLASAIVLTSQGIP
FLHAGQEFMRTKGGVENSYKSPIEVNWLDWERCAAHQDDVSYMRSLIALR
KAHPAFRLKTADEIRAHLRFEAAPPHTVAFTLRDHAGGDPDRHLYVLYNA
NPGALSLELPALGPWEVRFGGEHVLALEAARLEVRGVGVVVLAVPR
3D structure
PDB6jhi Crystal structure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose
ChainA
Resolution2.319 Å
3D
structure
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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 D409 R412 D401 R404
BS02 GLC A W234 Y236 H284 D350 E379 H469 W226 Y228 H276 D342 E371 H461
BS03 GLC A Y236 D237 N525 Y527 Y228 D229 N517 Y519
BS04 GLC A R495 D546 S549 R487 D538 S541
BS05 GLC A S553 G628 E630 S545 G620 E622
BS06 CA A D216 Y217 E224 E245 D208 Y209 E216 E237
BS07 CA A R364 D368 P372 R356 D360 P364
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

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Molecular Function
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Biological Process
External links
PDB RCSB:6jhi, PDBe:6jhi, PDBj:6jhi
PDBsum6jhi
PubMed
UniProtA0A0C5GWS2

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