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1J3U

Crystal structure of aspartase from Bacillus sp. YM55-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0006099biological_processtricarboxylic acid cycle
A0006531biological_processaspartate metabolic process
A0008797molecular_functionaspartate ammonia-lyase activity
A0016829molecular_functionlyase activity
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0006099biological_processtricarboxylic acid cycle
B0006531biological_processaspartate metabolic process
B0008797molecular_functionaspartate ammonia-lyase activity
B0016829molecular_functionlyase activity
Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN
ChainResidueDetails
AGLY317-ASN326

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsRegion: {"description":"SS loop","evidences":[{"source":"PubMed","id":"21661762","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"21661762","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21661762","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3R6V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
ATHR187
AHIS188
BSER318
BGLU331
BLYS324

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
AGLU331
ASER318
ALYS324
BTHR187
BHIS188

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PDB entries from 2025-12-17

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