1ZUW

Crystal structure of B.subtilis glutamate racemase (RacE) with D-Glu

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	14
Details	BINDING SITE FOR RESIDUE DGL A 1301

Chain	Residue
A	ASP10
A	CYS185
A	THR186
A	HIS187
A	HOH1318
A	HOH1326
A	SER11
A	PRO41
A	TYR42
A	GLY43
A	CYS74
A	ASN75
A	THR76
A	THR118

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE DGL B 2301

Chain	Residue
B	ASP10
B	SER11
B	PRO41
B	TYR42
B	GLY43
B	CYS74
B	ASN75
B	THR76
B	CYS185
B	THR186
B	HIS187
B	HOH2318
B	HOH2341

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DGL C 3301

Chain	Residue
C	ASP10
C	SER11
C	PRO41
C	TYR42
C	GLY43
C	CYS74
C	ASN75
C	THR76
C	THR118
C	CYS185
C	THR186
C	HIS187
C	HOH3302
C	HOH3304

---

Functional Information from PROSITE/UniProt

site_id	PS00923
Number of Residues	9
Details	ASP_GLU_RACEMASE_1 Aspartate and glutamate racemases signature 1. VIaC.NTATA

Chain	Residue	Details
A	VAL71-ALA79

---

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

Chain	Residue	Details
A	LEU181-LEU191

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-Rule:MF_00258

Chain	Residue	Details
A	CYS74
A	CYS185
B	CYS74
B	CYS185
C	CYS74
C	CYS185

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000269|PubMed:16271894, ECO:0007744|PDB:1ZUW

Chain	Residue	Details
A	ASP10
C	TYR42
C	ASN75
C	THR186
A	TYR42
A	ASN75
A	THR186
B	ASP10
B	TYR42
B	ASN75
B	THR186
C	ASP10

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1b73

Chain	Residue	Details
A	ASP10
A	CYS185
A	CYS74
A	SER11

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1b73

Chain	Residue	Details
B	ASP10
B	CYS185
B	CYS74
B	SER11

---

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1b73

Chain	Residue	Details
C	ASP10
C	CYS185
C	CYS74
C	SER11

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