Structure of PDB 3fha Chain B

Receptor sequence
>3fhaB (length=583) Species: 37930 (Glutamicibacter protophormiae) [Search protein sequence]
TYNGPLSSHWFPEELAQWEPDSDPDAPFNRSHVPLEPRVANRVNANADKD
AHLVSLSALNRHTSGVPSQGAPVFYENTFSYWHYTDLMVYWAGSAGEGII
VPPSADVIDASHRNGVPILGNVFFPPTVYGGQLEWLEQMLEQEEDGSFPL
ADKLLEVADYYGFDGWFINQETEGADEGTAEAMQAFLVYLQEQKPEGMHI
MWYDSMIDTGAIAWQNHLTDRNKMYLQNGSTRVADSMFLNFWWRDQRQSN
ELAQALGRSPYDLYAGVDVEARGTSTPVQWEGLFPEEKAHTSLGLYRPDW
AFQSSETMEAFYEKELQFWVGSTGNPAETDGQSNWPGMAHWFPAKSTATS
VPFVTHFNTGSGAQFSAEGKTVSEQEWNNRSLQDVLPTWRWIQHGGDLEA
TFSWEEAFEGGSSLQWHGSLAEGEHAQIELYQTELPLTWTFKSEHDNDLN
VGFRLDEEDFRYVEGEQRESINGWTQWTLQTITGLAFAAEGNGLAEFYTG
QLAVGSEKPAAPNVNVRQYDPDPSGIQLVWEKQSNVHHYRVYKEGKELIG
TSAGDRIYIEGLVRLHIEALSETFVPSDARMID
3D structure
PDB3fha Structural basis and catalytic mechanism for the dual functional endo-beta-N-acetylglucosaminidase A.
ChainB
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.96: mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase.
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 A366 E377 A363 E374
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033925 mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006517 protein deglycosylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:3fha, PDBe:3fha, PDBj:3fha
PDBsum3fha
PubMed19252736
UniProtQ9ZB22

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