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3R6Y

Crystal structure of chymotrypsin-treated aspartase from Bacillus sp. YM55-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
B0003824molecular_functioncatalytic activity
C0003824molecular_functioncatalytic activity
D0003824molecular_functioncatalytic activity
E0003824molecular_functioncatalytic activity
F0003824molecular_functioncatalytic activity
G0003824molecular_functioncatalytic activity
H0003824molecular_functioncatalytic activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA F 402
ChainResidue
FGLN339
FASN343
GASN343

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 402
ChainResidue
BASN343
BASN368
CGLN339
CASN343

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 Residues54
DetailsRegion: {"description":"SS loop","evidences":[{"source":"PubMed","id":"21661762","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"21661762","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues60
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21661762","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3R6V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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