1XPY

Structural Basis for Catalytic Racemization and Substrate Specificity of an N-Acylamino Acid Racemase Homologue from Deinococcus radiodurans

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009234	biological_process	menaquinone biosynthetic process
A	0016829	molecular_function	lyase activity
A	0016853	molecular_function	isomerase activity
A	0016854	molecular_function	racemase and epimerase activity
A	0043748	molecular_function	O-succinylbenzoate synthase activity
A	0046872	molecular_function	metal ion binding
B	0009234	biological_process	menaquinone biosynthetic process
B	0016829	molecular_function	lyase activity
B	0016853	molecular_function	isomerase activity
B	0016854	molecular_function	racemase and epimerase activity
B	0043748	molecular_function	O-succinylbenzoate synthase activity
B	0046872	molecular_function	metal ion binding
C	0009234	biological_process	menaquinone biosynthetic process
C	0016829	molecular_function	lyase activity
C	0016853	molecular_function	isomerase activity
C	0016854	molecular_function	racemase and epimerase activity
C	0043748	molecular_function	O-succinylbenzoate synthase activity
C	0046872	molecular_function	metal ion binding
D	0009234	biological_process	menaquinone biosynthetic process
D	0016829	molecular_function	lyase activity
D	0016853	molecular_function	isomerase activity
D	0016854	molecular_function	racemase and epimerase activity
D	0043748	molecular_function	O-succinylbenzoate synthase activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 1377

Chain	Residue
A	LYS168
A	ASP195
A	GLU220

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 2377

Chain	Residue
B	LYS168
B	ASP195
B	GLU220

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 3377

Chain	Residue
C	GLU220
C	ASP245
C	NLQ3376
C	LYS168
C	LYS170
C	ASP195

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 4377

Chain	Residue
D	LYS170
D	ASP195
D	ASN197
D	GLU220
D	ASP245
D	NLQ4376

---

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NLQ C 3376

Chain	Residue
C	PHE26
C	THR28
C	PHE30
C	SER142
C	LYS168
C	LYS170
C	ASP195
C	LYS269
C	GLY297
C	MET298
C	LEU299
C	ASP322
C	TYR329
C	MG3377
C	HOH3378
C	HOH3546

---

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE NLQ D 4376

Chain	Residue
D	PHE26
D	PHE30
D	SER142
D	LYS168
D	LYS170
D	LYS269
D	GLY297
D	MET298
D	LEU299
D	ASP322
D	TYR329
D	MG4377
D	HOH4412
D	HOH4445
D	HOH4555

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"15313614","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15313614","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15313614","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XPY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15313614","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XS2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GGH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15313614","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1r6w

Chain	Residue	Details
A	LYS269
A	LYS168

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1r6w

Chain	Residue	Details
B	LYS269
B	LYS168

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1r6w

Chain	Residue	Details
C	LYS269
C	LYS168

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1r6w

Chain	Residue	Details
D	LYS269
D	LYS168

---

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1r6w

Chain	Residue	Details
A	LYS170
A	LYS269

---

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1r6w

Chain	Residue	Details
B	LYS170
B	LYS269

---

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1r6w

Chain	Residue	Details
C	LYS170
C	LYS269

---

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1r6w

Chain	Residue	Details
D	LYS170
D	LYS269

---

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

---