Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6DHJ

Crystal structures of cyanuric acid hydrolase from Moorella thermoacetica

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016787	molecular_function	hydrolase activity
A	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A	0018753	molecular_function	cyanuric acid amidohydrolase activity
A	0019381	biological_process	atrazine catabolic process
A	0046872	molecular_function	metal ion binding
B	0016787	molecular_function	hydrolase activity
B	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
B	0018753	molecular_function	cyanuric acid amidohydrolase activity
B	0019381	biological_process	atrazine catabolic process
B	0046872	molecular_function	metal ion binding
C	0016787	molecular_function	hydrolase activity
C	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
C	0018753	molecular_function	cyanuric acid amidohydrolase activity
C	0019381	biological_process	atrazine catabolic process
C	0046872	molecular_function	metal ion binding
D	0016787	molecular_function	hydrolase activity
D	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
D	0018753	molecular_function	cyanuric acid amidohydrolase activity
D	0019381	biological_process	atrazine catabolic process
D	0046872	molecular_function	metal ion binding
E	0016787	molecular_function	hydrolase activity
E	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
E	0018753	molecular_function	cyanuric acid amidohydrolase activity
E	0019381	biological_process	atrazine catabolic process
E	0046872	molecular_function	metal ion binding
F	0016787	molecular_function	hydrolase activity
F	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
F	0018753	molecular_function	cyanuric acid amidohydrolase activity
F	0019381	biological_process	atrazine catabolic process
F	0046872	molecular_function	metal ion binding
G	0016787	molecular_function	hydrolase activity
G	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
G	0018753	molecular_function	cyanuric acid amidohydrolase activity
G	0019381	biological_process	atrazine catabolic process
G	0046872	molecular_function	metal ion binding
H	0016787	molecular_function	hydrolase activity
H	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
H	0018753	molecular_function	cyanuric acid amidohydrolase activity
H	0019381	biological_process	atrazine catabolic process
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue CIT A 401

Chain	Residue
A	GLY45
A	GLY348
A	ARG52
A	SER83
A	GLY84
A	ARG193
A	SER231
A	ALA232
A	ARG328
A	SER347

site_id	AC2
Number of Residues	10
Details	binding site for residue CIT F 401

Chain	Residue
F	GLY45
F	ARG52
F	SER83
F	GLY84
F	ARG193
F	SER231
F	ALA232
F	ARG328
F	SER347
F	GLY348

site_id	AC3
Number of Residues	12
Details	binding site for Di-peptide CIT B 401 and GLY B 84

Chain	Residue
B	LYS40
B	THR41
B	GLY45
B	ARG52
B	SER83
B	GLY85
B	ARG193
B	SER231
B	ALA232
B	ARG328
B	SER347
B	GLY348

site_id	AC4
Number of Residues	11
Details	binding site for Di-peptide CIT C 401 and GLY C 84

Chain	Residue
C	LYS40
C	THR41
C	GLY45
C	ARG52
C	SER83
C	GLY85
C	ARG193
C	SER231
C	ALA232
C	ARG328
C	GLY348

site_id	AC5
Number of Residues	20
Details	binding site for Di-peptide CIT D 401 and ARG D 328

Chain	Residue
D	ASN44
D	GLY45
D	ARG52
D	SER83
D	GLY84
D	GLY85
D	GLU87
D	ARG193
D	SER231
D	ALA232
D	THR324
D	ARG325
D	SER326
D	ALA327
D	ALA329
D	VAL330
D	VAL331
D	ASN332
D	SER347
D	GLY348

site_id	AC6
Number of Residues	12
Details	binding site for Di-peptide CIT D 401 and GLY D 348

Chain	Residue
D	GLY45
D	ARG52
D	SER83
D	GLY84
D	ARG193
D	SER231
D	ALA232
D	LYS299
D	ALA300
D	ARG328
D	SER347
D	GLY349

site_id	AC7
Number of Residues	12
Details	binding site for Di-peptide CIT E 401 and GLY E 45

Chain	Residue
E	GLY43
E	ASN44
E	SER46
E	ASP49
E	ARG52
E	SER83
E	GLY84
E	SER231
E	ALA232
E	ARG328
E	SER347
E	GLY348

site_id	AC8
Number of Residues	20
Details	binding site for Di-peptide CIT E 401 and ARG E 328

Chain	Residue
E	ALA327
E	ALA329
E	VAL330
E	VAL331
E	ASN332
E	VAL346
E	SER347
E	GLY348
E	GLY45
E	SER46
E	ASP49
E	ARG52
E	SER83
E	GLY84
E	GLU87
E	SER231
E	ALA232
E	THR324
E	ARG325
E	SER326

site_id	AC9
Number of Residues	18
Details	binding site for Di-peptide CIT G 401 and ARG G 193

Chain	Residue
G	GLY45
G	ARG52
G	SER83
G	GLY84
G	MET189
G	ALA190
G	TYR191
G	SER192
G	GLY194
G	ALA195
G	SER196
G	ALA197
G	THR230
G	SER231
G	ALA232
G	ARG328
G	GLY348
G	GLU351

site_id	AD1
Number of Residues	10
Details	binding site for Di-peptide ALA H 162 and ASN H 238

Chain	Residue
H	LYS161
H	PRO163
H	LEU164
H	SER196
H	SER231
H	ALA232
H	LEU236
H	LEU237
H	ASP239
H	GLU240

site_id	AD2
Number of Residues	8
Details	binding site for Di-peptide PRO H 163 and ASN H 238

Chain	Residue
H	LYS161
H	ALA162
H	LEU164
H	SER192
H	LEU236
H	LEU237
H	ASP239
H	GLU240

site_id	AD3
Number of Residues	8
Details	binding site for Di-peptide PRO H 163 and ASN H 238

Chain	Residue
H	LYS161
H	ALA162
H	LEU164
H	SER192
H	LEU236
H	LEU237
H	ASP239
H	GLU240

site_id	AD4
Number of Residues	19
Details	binding site for Di-peptide CIT H 401 and ARG H 328

Chain	Residue
H	ASN44
H	GLY45
H	ARG52
H	SER83
H	GLY84
H	GLY85
H	GLU87
H	ARG193
H	SER231
H	THR324
H	ARG325
H	SER326
H	ALA327
H	ALA329
H	VAL330
H	VAL331
H	ASN332
H	SER347
H	GLY348

site_id	AD5
Number of Residues	10
Details	binding site for Di-peptide CIT H 401 and GLY H 348

Chain	Residue
H	GLY45
H	ARG52
H	SER83
H	GLY84
H	ARG193
H	SER231
H	LYS299
H	ARG328
H	SER347
H	GLY349

site_id	AD6
Number of Residues	18
Details	binding site for Di-peptide CIT H 401 and ARG H 52

Chain	Residue
H	THR41
H	GLY45
H	SER46
H	ASP49
H	PHE50
H	THR51
H	CYS53
H	PHE54
H	ALA55
H	THR56
H	MET82
H	SER83
H	GLY84
H	ARG193
H	SER231
H	ARG328
H	SER347
H	GLY348

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_01989

Chain	Residue	Details
A	LYS161
B	LYS161
C	LYS161
D	LYS161
E	LYS161
F	LYS161
G	LYS161
H	LYS161

site_id	SWS_FT_FI2
Number of Residues	8
Details	ACT_SITE: Nucleophile => ECO:0000255\|HAMAP-Rule:MF_01989

Chain	Residue	Details
A	SER231
B	SER231
C	SER231
D	SER231
E	SER231
F	SER231
G	SER231
H	SER231

site_id	SWS_FT_FI3
Number of Residues	96
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01989

Chain	Residue	Details
A	ARG52
A	GLY359
A	PRO360
A	VAL363
B	ARG52
B	SER83
B	ARG193
B	SER231
B	GLY306
B	ALA333
B	HIS352
A	SER83
B	PRO355
B	GLY358
B	GLY359
B	PRO360
B	VAL363
C	ARG52
C	SER83
C	ARG193
C	SER231
C	GLY306
A	ARG193
C	ALA333
C	HIS352
C	PRO355
C	GLY358
C	GLY359
C	PRO360
C	VAL363
D	ARG52
D	SER83
D	ARG193
A	SER231
D	SER231
D	GLY306
D	ALA333
D	HIS352
D	PRO355
D	GLY358
D	GLY359
D	PRO360
D	VAL363
E	ARG52
A	GLY306
E	SER83
E	ARG193
E	SER231
E	GLY306
E	ALA333
E	HIS352
E	PRO355
E	GLY358
E	GLY359
E	PRO360
A	ALA333
E	VAL363
F	ARG52
F	SER83
F	ARG193
F	SER231
F	GLY306
F	ALA333
F	HIS352
F	PRO355
F	GLY358
A	HIS352
F	GLY359
F	PRO360
F	VAL363
G	ARG52
G	SER83
G	ARG193
G	SER231
G	GLY306
G	ALA333
G	HIS352
A	PRO355
G	PRO355
G	GLY358
G	GLY359
G	PRO360
G	VAL363
H	ARG52
H	SER83
H	ARG193
H	SER231
H	GLY306
A	GLY358
H	ALA333
H	HIS352
H	PRO355
H	GLY358
H	GLY359
H	PRO360
H	VAL363

site_id	SWS_FT_FI4
Number of Residues	8
Details	SITE: Important for substrate specificity => ECO:0000255\|HAMAP-Rule:MF_01989

Chain	Residue	Details
A	ALA329
B	ALA329
C	ALA329
D	ALA329
E	ALA329
F	ALA329
G	ALA329
H	ALA329

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)