Structure of PDB 3fhq Chain D

Receptor sequence
>3fhqD (length=597) Species: 37930 (Glutamicibacter protophormiae) [Search protein sequence]
TYNGPLSSHWFPEELAQWEPDSDPDAPFNRSHVPLEPGRVADRVNANADK
DAHLVSLSALNRHTSGVPSQGAPVFYENTFSYWHYTDLMVYWAGSAGEGI
IVPPSADVIDASHRNGVPILGNVFFPPTVYGGQLEWLEQMLEQEEDGSFP
LADKLLEVADYYGFDGWFINQETEGADEGTAEAMQAFLVYLQEQKPEGMH
IMWYDSMIDTGAIAWQNHLTDRNKMYLQNGSTRVADSMFLNFWWRDQRQS
NELAQALGRSPYDLYAGVDVEARGTSTPVQWEGLFPEEKAHTSLGLYRPD
WAFQSSETMEAFYEKELQFWVGSTGNPAETDGQSNWPGMAHWFPAKSTAT
SVPFVTHFNTGSGAQFSAEGKTVSEQEWNNRSLQDVLPTWRWIQHGGDLE
ATFSWEEAFEGGSSLQWHGSLAEGEHAQIELYQTELPISEGTSLTWTFKS
EHDNDLNVGFRLDDFRYVEGEQRESINGWTQWTLPLDAFAGQTITGLAFA
AEGNETGLAEFYTGQLAVGPAAPNVNVRQYDPDPSGIQLVWENVHHYRVY
KETKHGKELIGTSAGDRIYIEGLVEEVRLHIEALSETFVPSDARMID
3D structure
PDB3fhq Structural basis and catalytic mechanism for the dual functional endo-beta-N-acetylglucosaminidase A
ChainD
Resolution2.452 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 BMA D Y131 E272 Y299 Y130 E271 Y297
BS02 MAN D G95 S96 F125 Y131 G94 S95 F124 Y130
BS03 NGT D F169 N171 E173 Y205 F243 Y299 F168 N170 E172 Y204 F242 Y297
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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Biological Process
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Cellular Component
External links
PDB RCSB:3fhq, PDBe:3fhq, PDBj:3fhq
PDBsum3fhq
PubMed19252736
UniProtQ9ZB22

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