Structure of PDB 5goq Chain C

Receptor sequence
>5goqC (length=439) Species: 103690 (Nostoc sp. PCC 7120 = FACHB-418) [Search protein sequence]
LRETESWKLLESSIIYYEGNPIGTVAAQDPDQCFLRDFVPSAFVFLMDGQ
TDIVRNFLIETLTLQSHEKEMDCFQPGAGLMPASFKVESDGSKEYLVADF
GEKAIARVPPVDSCMWWILLLRAYEKATGDLTLAREPKFQAGIKLILDLC
LAHRFSMYPTMLVPDGAFMIDRRMGVYEHPLEIQVLFYAALRAARELLLP
DGDGEQYLNKVHGRLGALQYHIRNYYWVDLKRLREIYRYKGNEFGKEIAN
KFNIFSQSIPDWVIEWLPEKGGYLAGNLGPGRMDFRFFALGNLMAILAGL
ASEEESQRIMNLFAHRWEDLIGYMPVKICYPALQGLEWQIVTGCDPKNIP
WSYHNGGNWPVLLWLFTAAALKTGKVELAHEAIAIAEGRLSNDKFPEYYD
GNNGRLIGKEARIYQTWSIAGLLVAKQFLANPDHVEFIS
3D structure
PDB5goq Structural Analysis of the Catalytic Mechanism and Substrate Specificity of Anabaena Alkaline Invertase InvA Reveals a Novel Glucosidase
ChainC
Resolution2.75 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.26: beta-fructofuranosidase.
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 C F51 R53 D54 M186 D188 Y370 H371 F34 R36 D37 M169 D171 Y353 H354
Gene Ontology
Molecular Function
GO:0004564 beta-fructofuranosidase activity
GO:0004575 sucrose alpha-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033926 endo-alpha-N-acetylgalactosaminidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005987 sucrose catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5goq, PDBe:5goq, PDBj:5goq
PDBsum5goq
PubMed27777307
UniProtQ8YWS9

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