Structure of PDB 2yoc Chain A

Receptor sequence
>2yocA (length=1051) Species: 571 (Klebsiella oxytoca) [Search protein sequence]
DVVVRLPDVAVPGEAVTAVENQAVIHLVDIAGITSSSAADYSSKNLYLWN
NETCDALSAPVADWNDVSTTPSGSDKYGPYWVIPLNKESGCINVIVRDGT
DKLIDSDLRVAFGDFTDRTVSVIAGNSAVYDSRADAFRAAFGVALAEAHW
VDKNTLLWPGGQDKPIVRLYYSHSSKVAADGEGKFTDRYLKLTPTTVSQQ
VSMRFPHLSSYAAFKLPDNANVDELLQGETVAIAAAEDGILISATQVQTA
GVLDDAYAEAAEALSYGAQLADGGVTFRVWAPTAQQVDVVVYSADKKVIG
SHPMTRDSASGAWSWQGGSDLKGAFYRYAMTVYHPQSRKVEQYEVTDPYA
HSLSTNSEYSQVVDLNDSALKPDGWDNLTMPHAQKTKADLAKMTIHESHI
RDLSAWDQTVPAELRGKYLALTAGDSNMVQHLKTLSASGVTHVELLPVFD
LATVNEFSDKVADIQQPFSRLCEVNSAVKSSEFAGYCDSGSTVEEVLNQL
KQSDSQDNPQVQALNTLVAQTDSYNWGYDPFHYTVPEGSYATDPEGTTRI
KEFRTMIQAIKQDLGMNVIMDVVYNHTNAAGPTDRTSVLDKIVPWYYQRL
NETTGSVESATCCSDSAPEHRMFAKLIADSLAVWTTDYKIDGFRFDLMGY
HPKAQILSAWERIKALNPDIYFFGEGWDSNQSDRFEIASQINLKGTGIGT
FSDRLRDSVRGGGPFDSGDALRQNQGIGSGAGVLPNELASLSDDQVRHLA
DLTRLGMAGNLADFVMIDKDGAAKKGSEIDYNGAPGGYAADPTEVVNYVS
KHDNQTLWDMISYKASQEADLATRVRMQAVSLATVMLGQGIAFDQQGSEL
LRSKSFTRDSYDSGDWFNRVDYSLQDNNYNVGMPRISDDGSNYEVITRVK
EMVATPGEAELKQMTAFYQELTELRKSSPLFTLGDGSAVMKRVDFRNTGS
DQQAGLLVMTVDDGMKAGASLDSRLDGLVVAINAAPESRTLNEFAGETLQ
LSAIQQTAGENSLANGVQIAADGTVTLPAWSVAVLELPQGEAQGAGLPVS
S
3D structure
PDB2yoc Structural Basis of Pullulanase Membrane Binding and Secretion Revealed by X-Ray Crystallography, Molecular Dynamics and Biochemical Analysis
ChainA
Resolution2.88 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N375 D469 L470 E556 D665 E694 D822
Catalytic site (residue number reindexed from 1) N356 D450 L451 E537 D646 E675 D803
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 D469 L470 E475 E556 D450 L451 E456 E537
BS02 CA A A538 D541 Y543 D881 A519 D522 Y524 D862
BS03 CA A D982 S989 D991 L994 D995 Q1058 D963 S970 D972 L975 D976 Q1039
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
Cellular Component
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2yoc, PDBe:2yoc, PDBj:2yoc
PDBsum2yoc
PubMed26688215
UniProtP07206|PULA_KLEPN Pullulanase (Gene Name=pulA)

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