4L39

Crystal structure of GH3.12 from Arabidopsis thaliana in complex with AMPCPP and salicylate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0006952	biological_process	defense response
A	0009626	biological_process	plant-type hypersensitive response
A	0009863	biological_process	salicylic acid mediated signaling pathway
A	0010112	biological_process	regulation of systemic acquired resistance
A	0016046	biological_process	detection of fungus
A	0016874	molecular_function	ligase activity
A	0018874	biological_process	benzoate metabolic process
A	0034052	biological_process	positive regulation of plant-type hypersensitive response
A	0042742	biological_process	defense response to bacterium
A	0052625	molecular_function	4-aminobenzoate amino acid synthetase activity
A	0052626	molecular_function	benzoate amino acid synthetase activity
A	0052627	molecular_function	vanillate amino acid synthetase activity
A	0052628	molecular_function	4-hydroxybenzoate amino acid synthetase activity
A	0071456	biological_process	cellular response to hypoxia
B	0005515	molecular_function	protein binding
B	0006952	biological_process	defense response
B	0009626	biological_process	plant-type hypersensitive response
B	0009863	biological_process	salicylic acid mediated signaling pathway
B	0010112	biological_process	regulation of systemic acquired resistance
B	0016046	biological_process	detection of fungus
B	0016874	molecular_function	ligase activity
B	0018874	biological_process	benzoate metabolic process
B	0034052	biological_process	positive regulation of plant-type hypersensitive response
B	0042742	biological_process	defense response to bacterium
B	0052625	molecular_function	4-aminobenzoate amino acid synthetase activity
B	0052626	molecular_function	benzoate amino acid synthetase activity
B	0052627	molecular_function	vanillate amino acid synthetase activity
B	0052628	molecular_function	4-hydroxybenzoate amino acid synthetase activity
B	0071456	biological_process	cellular response to hypoxia

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 601

Chain	Residue
A	GLU329
A	VAL396
A	APC603

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SAL A 602

Chain	Residue
A	LEU116
A	TYR120
A	ARG123
A	THR324
A	GLY326

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site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE APC A 603

Chain	Residue
A	VAL299
A	THR301
A	THR324
A	GLY326
A	SER327
A	SER328
A	TYR347
A	ASP398
A	PHE414
A	MG601
A	HOH755
A	HOH766
A	SER95

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site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SAL B 601

Chain	Residue
B	TYR120
B	ARG123
B	ILE217
B	THR324
B	APC602

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site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE APC B 602

Chain	Residue
B	SER95
B	SER96
B	LYS104
B	THR301
B	THR324
B	TYR325
B	GLY326
B	SER327
B	SER328
B	TYR347
B	ASP398
B	LYS428
B	SAL601
B	HOH755
B	HOH765

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:22628555, ECO:0007744|PDB:4EPM, ECO:0007744|PDB:4EQ4, ECO:0007744|PDB:4EQL

Chain	Residue	Details
A	THR324
A	SER328
A	TYR347
A	ASP398
B	SER95
B	THR301
B	THR324
B	SER328
B	TYR347
B	ASP398
A	SER95
A	THR301

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:22628555, ECO:0007744|PDB:4EQ4, ECO:0007744|PDB:4EQL

Chain	Residue	Details
A	TYR120
B	TYR120

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:22628555, ECO:0007744|PDB:4EQ4

Chain	Residue	Details
A	ARG417
B	ARG417

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