Structure of PDB 7cb4 Chain B

Receptor sequence
>7cb4B (length=321) Species: 1648923 (Bacillus paralicheniformis) [Search protein sequence]
KKKVALITTGGTIASRKTESGRLAAGAISGPELAEMCSLPEDVQIDVYPA
FQLPSMHITFQHLLELKQTVERVFQDGSYDGVVVTHGTDTLEETAYFLDL
TLQDERPVVVTGSQRAPEQQGTDAYTNIRHAVYTACSPDIKGAGTVVVFN
ERIFNARYVKKVHASNLQGFDVFGFGYLGIIDNDKVYVYQKPLKRDVHQL
QRPLPEVDIVKCYLDGDGKFIRAAVREGAAGIVLEGVGRGQVPPNMVGDI
EQALHQGVYIVITTSAEEGEVYTTYDYAGSSYDLAKKGVILGKDYDSKKA
RMKLAVLLASYEEGIKDKFCY
3D structure
PDB7cb4 Structures of l-asparaginase from Bacillus licheniformis Reveal an Essential Residue for its Substrate Stereoselectivity.
ChainB
Resolution2.04 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T13 L24 E36 T89 D90 N156 K162 T274 A279 G280 S282
Catalytic site (residue number reindexed from 1) T12 L23 E35 T88 D89 N155 K161 T273 A278 G279 S281
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 B N246 D250 N245 D249
BS02 MG B E207 E228 E206 E227
Gene Ontology
Molecular Function
GO:0004067 asparaginase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0006528 asparagine metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:7cb4, PDBe:7cb4, PDBj:7cb4
PDBsum7cb4
PubMed33371681
UniProtA0A6I7U6Y2

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