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	8
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:21661762

Chain	Residue	Details
A	SER318
B	SER318
C	SER318
D	SER318
E	SER318
F	SER318
G	SER318
H	SER318

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site_id	SWS_FT_FI2
Number of Residues	64
Details	BINDING: BINDING => ECO:0000269|PubMed:21661762, ECO:0007744|PDB:3R6V

Chain	Residue	Details
A	THR101
B	SER140
B	THR141
B	ASN142
B	THR187
B	HIS188
B	SER319
B	LYS324
C	THR101
C	SER140
C	THR141
A	SER140
C	ASN142
C	THR187
C	HIS188
C	SER319
C	LYS324
D	THR101
D	SER140
D	THR141
D	ASN142
D	THR187
A	THR141
D	HIS188
D	SER319
D	LYS324
E	THR101
E	SER140
E	THR141
E	ASN142
E	THR187
E	HIS188
E	SER319
A	ASN142
E	LYS324
F	THR101
F	SER140
F	THR141
F	ASN142
F	THR187
F	HIS188
F	SER319
F	LYS324
G	THR101
A	THR187
G	SER140
G	THR141
G	ASN142
G	THR187
G	HIS188
G	SER319
G	LYS324
H	THR101
H	SER140
H	THR141
A	HIS188
H	ASN142
H	THR187
H	HIS188
H	SER319
H	LYS324
A	SER319
A	LYS324
B	THR101

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