Structure of PDB 4r4y Chain A

Receptor sequence
>4r4yA (length=293) Species: 172045 (Elizabethkingia miricola) [Search protein sequence]
NKPIVLSTWNFGLHANVEAWKVLSKGGKALDAVEKGVRLVEDDPTERSVG
YGGRPDRDGRVTLDACIMDENYNIGSVACMEHIKNPISVARAVMEKTPHV
MLVGDGALEFALSQGFKKENLLTAESEKEWKEWLKTSQYKPIVNIENHDT
IGMIALDAQGNLSGACTTSDMAYKMHGRVGDSPIIGAGLFVDNEIGAATA
TGHGEEVIRTVGTHLVVELMNQGRTPQQACKEAVERIVKIVNRRGKNLKD
IQVGFIALNKKGEYGAYCIQDGFNFAVHDQKGNRLETPGFALK
3D structure
PDB4r4y Structural Basis of a Point Mutation that Causes the Genetic Disease Aspartylglucosaminuria.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T152 T170 R180 T203 G204
Catalytic site (residue number reindexed from 1) T150 T168 R178 T201 G202
Enzyme Commision number 3.5.1.26: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase.
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 SD4 A H150 T152 D172 R180 D183 T203 G204 G206 H148 T150 D170 R178 D181 T201 G202 G204
Gene Ontology
Molecular Function
GO:0003948 N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
GO:0004067 asparaginase activity
GO:0008233 peptidase activity
GO:0008798 beta-aspartyl-peptidase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006508 proteolysis
GO:0006517 protein deglycosylation
Cellular Component
GO:0005737 cytoplasm
GO:0042597 periplasmic space

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Cellular Component
External links
PDB RCSB:4r4y, PDBe:4r4y, PDBj:4r4y
PDBsum4r4y
PubMed25456816
UniProtQ47898|ASPG_ELIMR N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase

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