Structure of PDB 2e8y Chain B

Receptor sequence
>2e8yB (length=712) Species: 1423 (Bacillus subtilis) [Search protein sequence]
MVSIRRSFEAYVDDMNIITVLIPAEQKEIMTPPFRLETEITDFPLAVREE
YSLEAKYKYVCVSDHPVTFGKIHCVRASSGHKTDLQIGAVIRTAAFDDEF
YYDGELGAVYTADHTVFKVWAPAATSAAVKLSHPNKSGRTFQMTRLEKGV
YAVTVTGDLHGYEYLFCICNNSEWMETVDQYAKAVTVNGEKGVVLRPDQM
KWTAPLKPFSHPVDAVIYETHLRDFSIHENSGMINKGKYLALTETDTQTA
NGSSSGLAYVKELGVTHVELLPVNDFAGVDEEKPLDAYNWGYNPLHFFAP
EGSYASNPHDPQTRKTELKQMINTLHQHGLRVILDVVFNHVYKRENSPFE
KTVPGYFFRHDECGKPSNGTGVGNDIASERRMARKFIADCVVYWLEEYNV
DGFRFDLLGILDIDTVLYMKEKATKAKPGILLFGEGWDLATPLPHEQKAA
LANAPRMPGIGFFNDMFRDAVKGNTFHLKATGFALGNGESAQAVMHGIAG
SSGWKALAPIVPEPSQSINYVESHDNHTFWDKMSFALPQENDSRKRSRQR
LAVAIILLAQGVPFIHSGQEFFRTKQGVENSYQSSDSINQLDWDRRETFK
EDVHYIRRLISLRKAHPAFRLRSAADIQRHLECLTLKEHLIAYRLYDLDE
VDEWKDIIVIHHASPDSVEWRLPNDIPYRLLCDPSGFQEDPTEIKKTVAV
NGIGTVILYLAS
3D structure
PDB2e8y Overexpression, purification and preliminary X-ray analysis of pullulanase from Bacillus subtilis strain 168
ChainB
Resolution2.11 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N188 D275 F276 E301 D406 E435 D525
Catalytic site (residue number reindexed from 1) N188 D275 F276 E301 D406 E435 D525
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 B D275 F276 E281 E301 D275 F276 E281 E301
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
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:2e8y, PDBe:2e8y, PDBj:2e8y
PDBsum2e8y
PubMed
UniProtC0SPA0|PULA_BACSU Pullulanase (Gene Name=amyX)

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