3OUT

Crystal structure of glutamate racemase from Francisella tularensis subsp. tularensis SCHU S4 in complex with D-glutamate.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008360	biological_process	regulation of cell shape
A	0008881	molecular_function	glutamate racemase activity
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016853	molecular_function	isomerase activity
A	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
A	0036361	molecular_function	racemase activity, acting on amino acids and derivatives
A	0071555	biological_process	cell wall organization
B	0008360	biological_process	regulation of cell shape
B	0008881	molecular_function	glutamate racemase activity
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0016853	molecular_function	isomerase activity
B	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
B	0036361	molecular_function	racemase activity, acting on amino acids and derivatives
B	0071555	biological_process	cell wall organization
C	0008360	biological_process	regulation of cell shape
C	0008881	molecular_function	glutamate racemase activity
C	0009252	biological_process	peptidoglycan biosynthetic process
C	0016853	molecular_function	isomerase activity
C	0016855	molecular_function	racemase and epimerase activity, acting on amino acids and derivatives
C	0036361	molecular_function	racemase activity, acting on amino acids and derivatives
C	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE DGL A 266

Chain	Residue
A	SER12
A	HOH271
A	HOH274
A	HOH285
A	HOH297
A	GLY13
A	PRO42
A	TYR43
A	GLY44
A	ASN75
A	THR76
A	CYS183
A	THR184

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site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DGL B 266

Chain	Residue
B	SER12
B	GLY13
B	PRO42
B	TYR43
B	GLY44
B	CYS74
B	ASN75
B	THR76
B	CYS183
B	THR184
B	HOH267
B	HOH279
B	HOH282
B	HOH285

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site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE DGL C 266

Chain	Residue
C	SER12
C	GLY13
C	PRO42
C	TYR43
C	GLY44
C	CYS74
C	ASN75
C	THR76
C	THR116
C	CYS183
C	THR184
C	HOH269
C	HOH280
C	HOH283
C	HOH299

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Functional Information from PROSITE/UniProt

site_id	PS00924
Number of Residues	11
Details	ASP_GLU_RACEMASE_2 Aspartate and glutamate racemases signature 2. LIlGCTHYPiI

Chain	Residue	Details
A	LEU179-ILE189

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