3R6Y

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
B	0003824	molecular_function	catalytic activity
C	0003824	molecular_function	catalytic activity
D	0003824	molecular_function	catalytic activity
E	0003824	molecular_function	catalytic activity
F	0003824	molecular_function	catalytic activity
G	0003824	molecular_function	catalytic activity
H	0003824	molecular_function	catalytic activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA F 402

Chain	Residue
F	GLN339
F	ASN343
G	ASN343

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 402

Chain	Residue
B	ASN343
B	ASN368
C	GLN339
C	ASN343

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Functional Information from PROSITE/UniProt

site_id	PS00163
Number of Residues	10
Details	FUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN

Chain	Residue	Details
A	GLY317-ASN326

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	54
Details	Region: {"description":"SS loop","evidences":[{"source":"PubMed","id":"21661762","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"21661762","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	60
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21661762","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3R6V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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