6AZS

Structural and biochemical characterization of a non-canonical biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016787	molecular_function	hydrolase activity
A	0018750	molecular_function	biuret amidohydrolase activity
B	0016787	molecular_function	hydrolase activity
B	0018750	molecular_function	biuret amidohydrolase activity
C	0016787	molecular_function	hydrolase activity
C	0018750	molecular_function	biuret amidohydrolase activity
D	0016787	molecular_function	hydrolase activity
D	0018750	molecular_function	biuret amidohydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue BTB A 301

Chain	Residue
A	ASN158
A	HOH486
B	ASN158
B	GLN159
B	ARG161
B	BTB301
A	ARG161
A	ILE162
A	GLU163
A	ARG186
A	GLY187
A	TYR188
A	HOH457
A	HOH464

---

site_id	AC2
Number of Residues	8
Details	binding site for residue GOL A 302

Chain	Residue
A	GLU154
A	ARG186
A	HOH489
A	HOH495
A	HOH522
A	HOH528
B	GLU154
D	ALA150

---

site_id	AC3
Number of Residues	4
Details	binding site for residue CL A 303

Chain	Residue
A	ASN8
A	ARG9
D	HOH458
D	HOH566

---

site_id	AC4
Number of Residues	14
Details	binding site for residue BTB B 301

Chain	Residue
A	ASN158
A	GLN159
A	ARG161
A	BTB301
B	ASN158
B	ARG161
B	ILE162
B	GLU163
B	ARG186
B	GLY187
B	TYR188
B	HOH421
B	HOH468
B	HOH489

---

site_id	AC5
Number of Residues	14
Details	binding site for residue BTB C 301

Chain	Residue
C	ASN158
C	ARG161
C	ILE162
C	GLU163
C	ARG186
C	GLY187
C	TYR188
C	HOH414
C	HOH467
C	HOH515
D	ASN158
D	GLN159
D	ARG161
D	BTB301

---

site_id	AC6
Number of Residues	9
Details	binding site for residue GOL C 302

Chain	Residue
B	ALA150
C	GLU154
C	ARG186
C	HOH402
C	HOH442
C	HOH450
D	GLU154
D	GOL304
D	HOH519

---

site_id	AC7
Number of Residues	14
Details	binding site for residue BTB D 301

Chain	Residue
C	ASN158
C	GLN159
C	ARG161
C	BTB301
D	ASN158
D	ARG161
D	ILE162
D	GLU163
D	ARG186
D	GLY187
D	TYR188
D	HOH424
D	HOH490
D	HOH492

---

site_id	AC8
Number of Residues	2
Details	binding site for residue PEG D 303

Chain	Residue
D	TYR202
D	TYR202

---

site_id	AC9
Number of Residues	9
Details	binding site for residue GOL D 304

Chain	Residue
A	ALA150
C	GLU154
C	GOL302
D	GLU154
D	ARG186
D	HOH414
D	HOH438
D	HOH502
D	HOH521

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"29425231","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PubMed","id":"29425231","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"29425231","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29425231","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6AZQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---