6AZQ

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
B	0016787	molecular_function	hydrolase activity
C	0016787	molecular_function	hydrolase activity
D	0016787	molecular_function	hydrolase activity
E	0016787	molecular_function	hydrolase activity
F	0016787	molecular_function	hydrolase activity
G	0016787	molecular_function	hydrolase activity
H	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue C5J G 301

Chain	Residue
G	ASP36
G	PHE41
G	GLU84
G	LYS145
G	ILE170
G	THR171
G	VAL174
G	SER175
H	GLN215

---

site_id	AC2
Number of Residues	1
Details	binding site for residue CA G 302

Chain	Residue
G	ARG186

---

site_id	AC3
Number of Residues	9
Details	binding site for residue C5J H 301

Chain	Residue
G	GLN215
H	ASP36
H	PHE41
H	GLU84
H	LYS145
H	ILE170
H	THR171
H	VAL174
H	SER175

---

site_id	AC4
Number of Residues	9
Details	binding site for residue C5J A 301

Chain	Residue
A	ASP36
A	PHE41
A	GLU84
A	LYS145
A	ILE170
A	THR171
A	VAL174
A	SER175
B	GLN215

---

site_id	AC5
Number of Residues	9
Details	binding site for residue C5J B 301

Chain	Residue
A	GLN215
B	ASP36
B	PHE41
B	GLU84
B	LYS145
B	ILE170
B	THR171
B	VAL174
B	SER175

---

site_id	AC6
Number of Residues	1
Details	binding site for residue CA B 302

Chain	Residue
B	ARG186

---

site_id	AC7
Number of Residues	9
Details	binding site for residue C5J C 301

Chain	Residue
C	ASP36
C	PHE41
C	GLU84
C	LYS145
C	ILE170
C	THR171
C	VAL174
C	SER175
D	GLN215

---

site_id	AC8
Number of Residues	2
Details	binding site for residue CA C 302

Chain	Residue
C	ARG186
C	HOH425

---

site_id	AC9
Number of Residues	1
Details	binding site for residue CA C 303

Chain	Residue
C	GLU130

---

site_id	AD1
Number of Residues	9
Details	binding site for residue C5J D 301

Chain	Residue
C	GLN215
D	ASP36
D	PHE41
D	GLU84
D	LYS145
D	ILE170
D	THR171
D	VAL174
D	SER175

---

site_id	AD2
Number of Residues	9
Details	binding site for residue C5J E 301

Chain	Residue
E	ASP36
E	PHE41
E	GLU84
E	LYS145
E	ILE170
E	THR171
E	VAL174
E	SER175
F	GLN215

---

site_id	AD3
Number of Residues	1
Details	binding site for residue CA F 301

Chain	Residue
F	ARG186

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:29425231

Chain	Residue	Details
G	ASP36
H	ASP36
A	ASP36
B	ASP36
C	ASP36
D	ASP36
E	ASP36
F	ASP36

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:29425231

Chain	Residue	Details
G	LYS142
H	LYS142
A	LYS142
B	LYS142
C	LYS142
D	LYS142
E	LYS142
F	LYS142

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:29425231

Chain	Residue	Details
G	SER175
H	SER175
A	SER175
B	SER175
C	SER175
D	SER175
E	SER175
F	SER175

---

site_id	SWS_FT_FI4
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269|PubMed:29425231, ECO:0007744|PDB:6AZQ

Chain	Residue	Details
G	GLU84
A	LYS145
A	ILE170
A	GLN215
B	GLU84
B	LYS145
B	ILE170
B	GLN215
C	GLU84
C	LYS145
C	ILE170
G	LYS145
C	GLN215
D	GLU84
D	LYS145
D	ILE170
D	GLN215
E	GLU84
E	LYS145
E	ILE170
E	GLN215
F	GLU84
G	ILE170
F	LYS145
F	ILE170
F	GLN215
G	GLN215
H	GLU84
H	LYS145
H	ILE170
H	GLN215
A	GLU84

---