Structure of PDB 2fh6 Chain A

Receptor sequence
>2fh6A (length=920) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
DVVVRLPAFGVALADAHWVDKTTLLWPGGENKPIVRLYYSHSSKVAADSN
GEFSDKYVKLTPTTVNQQVSMRFPHLASYPAFKLPDDVNVDELLQGETVA
IAAESDGILSSATQVQTAGVLDDTYAAAAEALSYGAQLTDSGVTFRVWAP
TAQQVELVIYSADKKVIASHPMTRDSASGAWSWQGGSDLKGAFYRYAMTV
YHPQSRKVEQYEVTDPYAHSLSTNSEYSQVVDLNDSALKPEGWDGLTMPH
AQKTKADLAKMTIHESHIRDLSAWDQTVPAELRGKYLALTAQESNMVQHL
KQLSASGVTHIELLPVFDLATVNEFSDKVADIQQPFSRLCEVNSAVKSSE
FAGYCDSGSTVEEVLTQLKQNDSKDNPQVQALNTLVAQTDSYNWGYDPFH
YTVPEGSYATDPEGTARIKEFRTMIQAIKQDLGMNVIMDVVYNHTNAAGP
TDRTSVLDKIVPWYYQRLNETTGSVESATCCSDSAPEHRMFAKLIADSLA
VWTTDYKIDGFRFDLMLYHPKAQILSAWERIKALNPDIYFFGEGWDSNQS
DRFEIASQINLKGTGIGTFSDRLRDAVRGGGPFDSGDALRQNQGVGSGAG
VLPNELTTLSDDQARHLADLTRLGMAGNLADFVLIDKDGAVKRGSEIDYN
GAPGGYAADPTEVVNYVSKHDNQTLWDMISYKAAQEADLDTRVRMQAVSL
ATVMLGQGIAFDQQGSELLRSKSFTRDSYDSGDWFNRVDYSLQDNNYNVG
MPRSSDDGSNYDIIARVKDAVATPGETELKQMTAFYQELTALRKSSPLFT
LGDGATVMKRVDFRNTGADQQTGLLVMTIDDGMQAGASLDSRVDGIVVAI
NAAPESRTLQDFAGTSLQLSAIQQAAGDRSLASGVQVAADGSVTLPAWSV
AVLELPQGESQGAGLPVSSK
3D structure
PDB2fh6 Crystal structure of pullulanase: evidence for parallel binding of oligosaccharides in the active site
ChainA
Resolution1.8 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 D560 D890 Y892 D397 D727 Y729
BS02 CA A A550 D553 Y555 D893 A387 D390 Y392 D730
BS03 CA A D994 S1001 D1003 S1004 V1006 Q1070 D831 S838 D840 S841 V843 Q907
BS04 CA A D481 L482 E487 E568 D318 L319 E324 E405
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate 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:2fh6, PDBe:2fh6, PDBj:2fh6
PDBsum2fh6
PubMed16650854
UniProtW9BQ28

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