2GGJ

The mutant Y218C of Deinococcus Radiodurans N-acylamino acid racemase

Replaces:  2FKTReplaces:  2BAE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0009234	biological_process	menaquinone biosynthetic process
A	0016829	molecular_function	lyase activity
A	0016853	molecular_function	isomerase activity
A	0043748	molecular_function	O-succinylbenzoate synthase activity
A	0046872	molecular_function	metal ion binding
B	0003824	molecular_function	catalytic activity
B	0009234	biological_process	menaquinone biosynthetic process
B	0016829	molecular_function	lyase activity
B	0016853	molecular_function	isomerase activity
B	0043748	molecular_function	O-succinylbenzoate synthase activity
B	0046872	molecular_function	metal ion binding
C	0003824	molecular_function	catalytic activity
C	0009234	biological_process	menaquinone biosynthetic process
C	0016829	molecular_function	lyase activity
C	0016853	molecular_function	isomerase activity
C	0043748	molecular_function	O-succinylbenzoate synthase activity
C	0046872	molecular_function	metal ion binding
D	0003824	molecular_function	catalytic activity
D	0009234	biological_process	menaquinone biosynthetic process
D	0016829	molecular_function	lyase activity
D	0016853	molecular_function	isomerase activity
D	0043748	molecular_function	O-succinylbenzoate synthase activity
D	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:15313614

Chain	Residue	Details
A	LYS170
B	LYS170
C	LYS170
D	LYS170

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:15313614

Chain	Residue	Details
A	LYS269
B	LYS269
C	LYS269
D	LYS269

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269|PubMed:15313614, ECO:0007744|PDB:1XPY

Chain	Residue	Details
C	SER142
C	LYS168
C	LYS269
C	LEU299
D	SER142
D	LYS168
D	LYS269
D	LEU299
A	SER142
A	LYS168
A	LYS269
A	LEU299
B	SER142
B	LYS168
B	LYS269
B	LEU299

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:15313614, ECO:0007744|PDB:1XPY, ECO:0007744|PDB:1XS2, ECO:0007744|PDB:2GGH

Chain	Residue	Details
C	ASP195
C	GLU220
D	ASP195
D	GLU220
A	ASP195
A	GLU220
B	ASP195
B	GLU220

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15313614

Chain	Residue	Details
A	ASP245
B	ASP245
C	ASP245
D	ASP245

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	8
Details	M-CSA 377

Chain	Residue	Details
A	SER142	transition state stabiliser
A	LYS168	transition state stabiliser
A	LYS170	proton donor
A	ASP195	metal ligand
A	GLU220	metal ligand
A	ASP245	metal ligand
A	LYS269	proton acceptor
A	GLY297	transition state stabiliser

---

site_id	MCSA2
Number of Residues	8
Details	M-CSA 377

Chain	Residue	Details
B	SER142	transition state stabiliser
B	LYS168	transition state stabiliser
B	LYS170	proton donor
B	ASP195	metal ligand
B	GLU220	metal ligand
B	ASP245	metal ligand
B	LYS269	proton acceptor
B	GLY297	transition state stabiliser

---

site_id	MCSA3
Number of Residues	8
Details	M-CSA 377

Chain	Residue	Details
C	SER142	transition state stabiliser
C	LYS168	transition state stabiliser
C	LYS170	proton donor
C	ASP195	metal ligand
C	GLU220	metal ligand
C	ASP245	metal ligand
C	LYS269	proton acceptor
C	GLY297	transition state stabiliser

---

site_id	MCSA4
Number of Residues	8
Details	M-CSA 377

Chain	Residue	Details
D	SER142	transition state stabiliser
D	LYS168	transition state stabiliser
D	LYS170	proton donor
D	ASP195	metal ligand
D	GLU220	metal ligand
D	ASP245	metal ligand
D	LYS269	proton acceptor
D	GLY297	transition state stabiliser

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