5HXZ

Structure-function analysis of functionally diverse members of the cyclic amide hydrolase family of Toblerone fold enzymes

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006212	biological_process	uracil catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A	0046872	molecular_function	metal ion binding
A	0047694	molecular_function	barbiturase activity
B	0006212	biological_process	uracil catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
B	0046872	molecular_function	metal ion binding
B	0047694	molecular_function	barbiturase activity
C	0006212	biological_process	uracil catabolic process
C	0016787	molecular_function	hydrolase activity
C	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
C	0046872	molecular_function	metal ion binding
C	0047694	molecular_function	barbiturase activity
D	0006212	biological_process	uracil catabolic process
D	0016787	molecular_function	hydrolase activity
D	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
D	0046872	molecular_function	metal ion binding
D	0047694	molecular_function	barbiturase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue CL A 401

Chain	Residue
A	ARG34
A	ALA102

---

site_id	AC2
Number of Residues	1
Details	binding site for residue CL A 402

Chain	Residue
A	ARG254

---

site_id	AC3
Number of Residues	14
Details	binding site for residue MHA A 403

Chain	Residue
A	LYS162
A	MET190
A	ASN194
A	SER230
A	SER231
A	LYS328
A	SER347
A	VAL348
A	GLY46
A	GLY47
A	ASP50
A	ARG53
A	SER83
A	GLY84

---

site_id	AC4
Number of Residues	6
Details	binding site for residue NA A 404

Chain	Residue
A	GLU301
A	ALA350
A	GLN353
A	GLY354
A	PRO355
A	GLY358

---

site_id	AC5
Number of Residues	1
Details	binding site for residue CL B 401

Chain	Residue
B	ARG34

---

site_id	AC6
Number of Residues	6
Details	binding site for residue NA B 402

Chain	Residue
B	GLU301
B	ALA350
B	GLN353
B	GLY354
B	PRO355
B	GLY358

---

site_id	AC7
Number of Residues	6
Details	binding site for residue NA C 401

Chain	Residue
C	GLU301
C	ALA350
C	GLN353
C	GLY354
C	PRO355
C	GLY358

---

site_id	AC8
Number of Residues	14
Details	binding site for residue MHA D 402

Chain	Residue
D	GLY46
D	ARG53
D	TRP82
D	SER83
D	GLY84
D	LYS162
D	MET190
D	ASN194
D	SER230
D	SER231
D	LYS299
D	LYS328
D	SER347
D	VAL348

---

site_id	AC9
Number of Residues	6
Details	binding site for residue NA D 403

Chain	Residue
D	GLU301
D	ALA350
D	GLN353
D	GLY354
D	PRO355
D	GLY358

---

Functional Information from PROSITE/UniProt

site_id	PS00136
Number of Residues	12
Details	SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. AKLIDDGVleaD

Chain	Residue	Details
A	ALA22-ASP33

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01989

Chain	Residue	Details
A	LYS162
B	LYS162
C	LYS162
D	LYS162

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01989

Chain	Residue	Details
A	SER230
B	SER230
C	SER230
D	SER230

---

site_id	SWS_FT_FI3
Number of Residues	48
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:28235873

Chain	Residue	Details
A	ARG53
A	GLY354
A	PRO355
A	GLY358
B	ARG53
B	SER83
B	ASN194
B	SER230
B	GLU301
B	LYS328
B	SER347
A	SER83
B	ALA350
B	GLN353
B	GLY354
B	PRO355
B	GLY358
C	ARG53
C	SER83
C	ASN194
C	SER230
C	GLU301
A	ASN194
C	LYS328
C	SER347
C	ALA350
C	GLN353
C	GLY354
C	PRO355
C	GLY358
D	ARG53
D	SER83
D	ASN194
A	SER230
D	SER230
D	GLU301
D	LYS328
D	SER347
D	ALA350
D	GLN353
D	GLY354
D	PRO355
D	GLY358
A	GLU301
A	LYS328
A	SER347
A	ALA350
A	GLN353

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Important for substrate specificity => ECO:0000255|HAMAP-Rule:MF_01989

Chain	Residue	Details
A	HIS324
B	HIS324
C	HIS324
D	HIS324

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