Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:21661762
ChainResidueDetails
ASER318
BSER318

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:21661762, ECO:0007744|PDB:3R6V
ChainResidueDetails
ATHR101
BSER140
BTHR141
BASN142
BTHR187
BHIS188
BSER319
BLYS324
ASER140
ATHR141
AASN142
ATHR187
AHIS188
ASER319
ALYS324
BTHR101

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

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon