2OKK

The X-ray crystal structure of the 65kDa isoform of Glutamic Acid Decarboxylase (GAD65)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016830	molecular_function	carbon-carbon lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ABU A 585

Chain	Residue
A	GLN181
A	LEU182
A	SER183
A	PHE205
A	THR339
A	ARG558

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ABU A 586

Chain	Residue
A	ASN203
A	HIS282
A	LLP396
A	CYS446
A	HOH661
A	GLN181
A	LEU182
A	SER183

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 587

Chain	Residue
A	GLU279
A	SER281
A	HIS282
A	PHE283
A	LYS286

---

Functional Information from PROSITE/UniProt

site_id	PS00392
Number of Residues	22
Details	DDC_GAD_HDC_YDC DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site. SVtWnphKMMgVpLQCsaLLvR

Chain	Residue	Details
A	SER389-ARG410

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17384644","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ecx

Chain	Residue	Details
A	ASP364
A	HIS282

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ecx

Chain	Residue	Details
A	HIS280
A	ASP364

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ecx

Chain	Residue	Details
A	ASP364
A	PHE283

---