Structure of PDB 2fgz Chain A

Receptor sequence
>2fgzA (length=926) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
DVVVRLPDDAFRAAFGVALADAHWVDKTTLLWPGGENKPIVRLYYSHSSK
VAADSNGEFSDKYVKLTPTTVNQQVSMRFPHLASYPAFKLPDDVNVDELL
QGETVAIAAESDGILSSATQVQTAGVLDDTYAAAAEALSYGAQLTDSGVT
FRVWAPTAQQVELVIYSADKKVIASHPMTRDSASGAWSWQGGSDLKGAFY
RYAMTVYHPQSRKVEQYEVTDPYAHSLSTNSEYSQVVDLNDSALKPEGWD
GLTMPHAQKTKADLAKMTIHESHIRDLSAWDQTVPAELRGKYLALTAQES
NMVQHLKQLSASGVTHIELLPVFDLATVNEFSDKVADIQQPFSRLCEVNS
AVKSSEFAGYCDSGSTVEEVLTQLKQNDSKDNPQVQALNTLVAQTDSYNW
GYDPFHYTVPEGSYATDPEGTARIKEFRTMIQAIKQDLGMNVIMDVVYNH
TNAAGPTDRTSVLDKIVPWYYQRLNETTGSVESATCCSDSAPEHRMFAKL
IADSLAVWTTDYKIDGFRFDLMLYHPKAQILSAWERIKALNPDIYFFGEG
WDSNQSDRFEIASQINLKGTGIGTFSDRLRDAVRGGGPFDSGDALRQNQG
VGSGAGVLPNELTTLSDDQARHLADLTRLGMAGNLADFVLIDKDGAVKRG
SEIDYNGAPGGYAADPTEVVNYVSKHDNQTLWDMISYKAAQEADLDTRVR
MQAVSLATVMLGQGIAFDQQGSELLRSKSFTRDSYDSGDWFNRVDYSLQD
NNYNVGMPRSSDDGSNYDIIARVKDAVATPGETELKQMTAFYQELTALRK
SSPLFTLGDGATVMKRVDFRNTGADQQTGLLVMTIDDGMQAGASLDSRVD
GIVVAINAAPESRTLQDFAGTSLQLSAIQQAAGDRSLASGVQVAADGSVT
LPAWSVAVLELPQGESQGAGLPVSSK
3D structure
PDB2fgz Crystal structure of pullulanase: evidence for parallel binding of oligosaccharides in the active site
ChainA
Resolution1.75 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 CA A A550 D553 Y555 D893 A393 D396 Y398 D736
BS02 CA A D994 S1001 D1003 V1006 Q1070 D837 S844 D846 V849 Q913
BS03 CA A D481 L482 E487 E568 D324 L325 E330 E411
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:2fgz, PDBe:2fgz, PDBj:2fgz
PDBsum2fgz
PubMed16650854
UniProtW9BQ28

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