Structure of PDB 1gye Chain B

Receptor sequence
>1gyeB (length=315) Species: 155077 (Cellvibrio japonicus) [Search protein sequence]
KQVDVHDPVMTREGATWYLFSTGPGITIYSSKDRVNWRYSDRAFATEPTW
AKRVSPSFDGHLWAPDIYQHKGLFYLYYSVSAFGKNTSAIGVTVNKTLNP
ASPDYRWEDKGIVIESVPQRDLWNAIAPAIIADDHGQVWMSFGSFWGGLK
LFKLNDDLTRPAEPQEWHSIAKLERSVLMDDSQAGSAQIEAPFILRKGDY
YYLFASWGLCCRKGDSTYHLVVGRSKQVTGPYLDKTGRDMNQGGGSLLIK
GNKRWVGLGHNSAYTWDGKDYLVLHAYEAADNYLQKLKILNLHWDGEGWP
QVDEKELDSYISQRL
3D structure
PDB1gye Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-propeller fold.
ChainB
Resolution2.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.55: non-reducing end alpha-L-arabinofuranosidase.
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 AHR B F114 G115 S175 F176 F83 G84 S144 F145
BS02 AHR B W94 E221 W63 E190
BS03 AHR B D35 V36 T53 G54 Q316 D4 V5 T22 G23 Q285
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046556 alpha-L-arabinofuranosidase activity
GO:0046558 arabinan endo-1,5-alpha-L-arabinosidase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0031222 arabinan catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1gye, PDBe:1gye, PDBj:1gye
PDBsum1gye
PubMed12198486
UniProtP95470|ARBA_CELJU Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA (Gene Name=arbA)

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