Structure of PDB 9gac Chain A

Receptor sequence
>9gacA (length=280) Species: 238 (Elizabethkingia meningoseptica) [Search protein sequence]
TNKPIVLSTWNFGLHANVEAWKVLSKGGKALDAVEKGVRLVEDDPTERSV
GYGGRPDRDGRVTLDACIMDENYNIGSVACMEHIKNPISVARAVMEKTPH
VMLVGDGALEFALSQGFKKENLLTAESEKEWKEWLHDCIGMIALDAQGNL
SGACTTSGMAYKMHGRVGDSPIIGAGLFVDNEIGAATATGHGEEVIRTVG
THLVVELMNQGRTPQQACKEAVERIVKIVNRRGKNLKDIQVGFIALNKKG
EYGAYCIQDGFNFAVHDQKGNRLETPGFAL
3D structure
PDB9gac Structural insights into the mechanism of intramolecular proteolysis.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) C152
Catalytic site (residue number reindexed from 1) C138
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 GLY A D151 R180 D183 G204 G206 D137 R166 D169 G190 G192
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:9gac, PDBe:9gac, PDBj:9gac
PDBsum9gac
PubMed10490104
UniProtQ47898|ASPG_ELIMR N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase

[Back to BioLiP]