Structure of PDB 3fha Chain A

Receptor sequence

>3fhaA (length=598) Species: 37930 (Glutamicibacter protophormiae)

TYNGPLSSHWFPEELAQWEPDSDPDAPFNRSHVPLEPGRVANRVNANADK
DAHLVSLSALNRHTSGVPSQGAPVFYENTFSYWHYTDLMVYWAGSAGEGI
IVPPSADVIDASHRNGVPILGNVFFPPTVYGGQLEWLEQMLEQEEDGSFP
LADKLLEVADYYGFDGWFINQETEGADEGTAEAMQAFLVYLQEQKPEGMH
IMWYDSMIDTGAIAWQNHLTDRNKMYLQNGSTRVADSMFLNFWWRDQRQS
NELAQALGRSPYDLYAGVDVEARGTSTPVQWEGLFPEEKAHTSLGLYRPD
WAFQSSETMEAFYEKELQFWVGSTGNPAETDGQSNWPGMAHWFPAKSTAT
SVPFVTHFNTGSGAQFSAEGKTVSEQEWNNRSLQDVLPTWRWIQHGGDLE
ATFSWEEAFEGGSSLQWHGSLAEGEHAQIELYQTELPISEGTSLTWTFKS
EHDNDLNVGFRLDGEEDFRYVEGEQRESINGWTQWTLPLDAFAGQTITGL
AFAAEGNETGLAEFYTGQLAVGPAAPNVNVRQYDPDPSGIQLVWENVHHY
RVYKETKHGKELIGTSAGDRIYIEGLEVRLHIEALSETFVPSDARMID

3D structure

• PDB: 3fha Structural basis and catalytic mechanism for the dual functional endo-beta-N-acetylglucosaminidase A.
• Chain: A
• Resolution: 2.0 Å

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	A	A366 E377	A364 E375

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

External links

• PDB: RCSB:3fha, PDBe:3fha, PDBj:3fha
• PDBsum: 3fha
• PubMed: 19252736
• UniProt: Q9ZB22