5FJU

N-acyl amino acid racemase from Amycolatopsis sp. Ts-1-60: Q26A M50I G291D F323Y mutant in complex with N-acetyl phenylalanine

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	6
Details	BINDING SITE FOR RESIDUE MG B 1368

Chain	Residue
B	ASP189
B	ASN191
B	GLU214
B	ASP239
B	GLU240
B	5CR1369

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 1368

Chain	Residue
C	ASP239
C	GLU240
C	5CR1370
C	ASP189
C	ASN191
C	GLU214

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG D 1368

Chain	Residue
D	ASP189
D	ASN191
D	GLU214
D	ASP239
D	GLU240
D	5CR1370
D	HOH2063

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1369

Chain	Residue
A	ASP189
A	ASN191
A	GLU214
A	ASP239
A	5CR1370

---

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 5CR A 1370

Chain	Residue
A	PHE19
A	ILE50
A	SER135
A	LYS161
A	LYS163
A	ASP189
A	ASN191
A	GLU214
A	ASP239
A	LYS263
A	ASP291
A	MET292
A	TYR323
A	MG1369

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 5CR C 1369

Chain	Residue
C	GLY24
C	VAL28
C	ILE50
C	ALA51
C	GLY52

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 5CR D 1369

Chain	Residue
D	GLY24
D	THR25
D	VAL28
D	GLU30
D	ILE50
D	ALA51
D	GLY52

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 5CR A 1371

Chain	Residue
A	THR25
A	ALA26
A	VAL28
A	ILE50
A	ALA51
A	GLY52

---

site_id	AC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 5CR D 1370

Chain	Residue
D	PHE19
D	ILE50
D	SER135
D	LYS161
D	LYS163
D	ASP189
D	ASN191
D	ASP239
D	LYS263
D	ASP291
D	MET292
D	ILE293
D	ASP316
D	TYR323
D	MG1368
D	HOH2063

---

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 5CR C 1370

Chain	Residue
C	PHE19
C	ILE50
C	SER135
C	LYS161
C	LYS163
C	ASP189
C	ASN191
C	GLU214
C	ASP239
C	LYS263
C	ASP291
C	MET292
C	ILE293
C	ASP316
C	TYR323
C	MG1368

---

site_id	BC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 5CR B 1369

Chain	Residue
B	MET292
B	ILE293
B	TYR323
B	MG1368
B	PHE19
B	ILE50
B	SER135
B	LYS161
B	LYS163
B	ASP189
B	ASN191
B	GLU214
B	ASP239
B	LYS263
B	ASP291

---

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 5CR B 1370

Chain	Residue
B	PHE23
B	GLY24
B	VAL28
B	ILE50
B	ALA51
B	GLY52
B	HOH2011

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"14705949","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15134446","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":"14705949","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15134446","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15134446","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SJB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15134446","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23130969","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2015","submissionDatabase":"PDB data bank","title":"Structure of N-Acylamino Acid Racemase Mutants in Complex with Substrates.","authors":["Sanchez-Carron G.","Campopiano D.","Grogan G."]}},{"source":"PDB","id":"1SJA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SJB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SJC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A6G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FJO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FJP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FJR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FJT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FJU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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