Structure of PDB 5k4g Chain C

Receptor sequence
>5k4gC (length=328) Species: 273121 (Wolinella succinogenes DSM 1740) [Search protein sequence]
KPQVTILATGGTIAGSGESSVKSSYSAGAVTVDKLLAAVPAINDLATIKG
EQISSIGSQEMTGKVWLKLAKRVNELLAQKETEAVIITHGTDTMEETAFF
LNLTVKSQKPVVLVGAMRSGSSMSADGPMNLYNAVNVAINKASTNKGVVI
VMNDEIHAAREATKLNTTAVNAFASPNTGKIGTVYYGKVEYFTQSVRPHT
LASEFDISKIEELPRVDILYAHPDDTDVLVNAALQAGAKGIIHAGMGNGN
PFPLTQNALEKAAKSGVVVARSSRVGSGSTTQEAEVDDKKLGFVATESLN
PQKARVLLMLALTKTSDREAIQKIFSTY
3D structure
PDB5k4g The differential ability of asparagine and glutamine in promoting the closed/active enzyme conformation rationalizes the Wolinella succinogenes L-asparaginase substrate specificity.
ChainC
Resolution1.6 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) T14 Y27 T93 D94 K166 E287
Catalytic site (residue number reindexed from 1) T12 Y25 T91 D92 K164 E285
Enzyme Commision number 3.5.1.1: 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 ASP C G59 S60 Q61 G92 T93 D94 A118 G57 S58 Q59 G90 T91 D92 A116
Gene Ontology
Molecular Function
GO:0004067 asparaginase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0006528 asparagine metabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5k4g, PDBe:5k4g, PDBj:5k4g
PDBsum5k4g
PubMed28139703
UniProtP50286|ASPG_WOLSU L-asparaginase (Gene Name=ansA)

[Back to BioLiP]