1XWO

crystal structrue of goose delta crystallin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004056	molecular_function	argininosuccinate lyase activity
A	0005212	molecular_function	structural constituent of eye lens
A	0005829	cellular_component	cytosol
A	0006526	biological_process	L-arginine biosynthetic process
A	0016829	molecular_function	lyase activity
A	0042450	biological_process	arginine biosynthetic process via ornithine
B	0003824	molecular_function	catalytic activity
B	0004056	molecular_function	argininosuccinate lyase activity
B	0005212	molecular_function	structural constituent of eye lens
B	0005829	cellular_component	cytosol
B	0006526	biological_process	L-arginine biosynthetic process
B	0016829	molecular_function	lyase activity
B	0042450	biological_process	arginine biosynthetic process via ornithine
C	0003824	molecular_function	catalytic activity
C	0004056	molecular_function	argininosuccinate lyase activity
C	0005212	molecular_function	structural constituent of eye lens
C	0005829	cellular_component	cytosol
C	0006526	biological_process	L-arginine biosynthetic process
C	0016829	molecular_function	lyase activity
C	0042450	biological_process	arginine biosynthetic process via ornithine
D	0003824	molecular_function	catalytic activity
D	0004056	molecular_function	argininosuccinate lyase activity
D	0005212	molecular_function	structural constituent of eye lens
D	0005829	cellular_component	cytosol
D	0006526	biological_process	L-arginine biosynthetic process
D	0016829	molecular_function	lyase activity
D	0042450	biological_process	arginine biosynthetic process via ornithine

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY280-ASN289

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P24058

Chain	Residue	Details
A	HIS160
B	HIS160
C	HIS160
D	HIS160

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site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P24058

Chain	Residue	Details
A	SER281
B	SER281
C	SER281
D	SER281

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: in chain A => ECO:0000250|UniProtKB:P24058

Chain	Residue	Details
A	SER27
B	LYS329
C	SER27
C	ASN114
C	TYR321
C	GLN326
C	LYS329
D	SER27
D	ASN114
D	TYR321
D	GLN326
A	ASN114
D	LYS329
A	TYR321
A	GLN326
A	LYS329
B	SER27
B	ASN114
B	TYR321
B	GLN326

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: in chain C => ECO:0000250|UniProtKB:P24058

Chain	Residue	Details
A	THR159
B	THR159
C	THR159
D	THR159

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: in chain B => ECO:0000250|UniProtKB:P24058

Chain	Residue	Details
A	ASN289
B	ASN289
C	ASN289
D	ASN289

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	SITE: Increases basicity of active site His => ECO:0000250|UniProtKB:P24058

Chain	Residue	Details
A	GLU294
B	GLU294
C	GLU294
D	GLU294

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1auw

Chain	Residue	Details
A	HIS160
A	THR159
B	SER281
B	LYS287
B	GLU294

---

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1auw

Chain	Residue	Details
A	SER281
A	LYS287
A	GLU294
B	HIS160
B	THR159

---

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1auw

Chain	Residue	Details
C	HIS160
C	THR159
D	SER281
D	LYS287
D	GLU294

---

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1auw

Chain	Residue	Details
C	SER281
C	LYS287
C	GLU294
D	HIS160
D	THR159

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