Structure of PDB 7cbu Chain A

Receptor sequence
>7cbuA (length=318) Species: 1648923 (Bacillus paralicheniformis) [Search protein sequence]
KKKVALITTGGAIASRKGRLAAGAISGPELAEMCSLPEDVQIDVYPAFQL
PSMHITFQHLLELKQTVERVFQDGSYDGVVVTHGTDTLEETAYFLDLTLQ
DERPVVVTGSQRAPEQQGTDAYTNIRHAVYTACSPDIKGAGTVVVFNERI
FNARYVKKVHASNLQGFDVFGFGYLGIIDNDKVYVYQKPLKRDVHQLQRP
LPEVDIVKCYLDGDGKFIRAAVREGAAGIVLEGVGRGQVPPNMVGDIEQA
LHQGVYIVITTSAEEGEVYTTYDYAGSSYDLAKKGVILGKDYDSKKARMK
LAVLLASYEEGIKDKFCY
3D structure
PDB7cbu Structures of l-asparaginase from Bacillus licheniformis Reveal an Essential Residue for its Substrate Stereoselectivity.
ChainA
Resolution2.25 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) A13 L24 E36 T89 D90 N156 K162 T274 A279 G280 S282
Catalytic site (residue number reindexed from 1) A12 L20 E32 T85 D86 N152 K158 T270 A275 G276 S278
Enzyme Commision number ?
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 MG A N246 D250 N242 D246
BS02 ASP A A13 S56 G88 T89 D90 A12 S52 G84 T85 D86
Gene Ontology
Molecular Function
GO:0004067 asparaginase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006528 asparagine metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7cbu, PDBe:7cbu, PDBj:7cbu
PDBsum7cbu
PubMed33371681
UniProtA0A6I7U6Y2

[Back to BioLiP]