Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4V1Y

The structure of the hexameric atrazine chlorohydrolase, AtzA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0016787	molecular_function	hydrolase activity
A	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A	0018788	molecular_function	atrazine chlorohydrolase activity
A	0019381	biological_process	atrazine catabolic process
A	0046872	molecular_function	metal ion binding
B	0005737	cellular_component	cytoplasm
B	0016787	molecular_function	hydrolase activity
B	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B	0018788	molecular_function	atrazine chlorohydrolase activity
B	0019381	biological_process	atrazine catabolic process
B	0046872	molecular_function	metal ion binding
C	0005737	cellular_component	cytoplasm
C	0016787	molecular_function	hydrolase activity
C	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C	0018788	molecular_function	atrazine chlorohydrolase activity
C	0019381	biological_process	atrazine catabolic process
C	0046872	molecular_function	metal ion binding
D	0005737	cellular_component	cytoplasm
D	0016787	molecular_function	hydrolase activity
D	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
D	0018788	molecular_function	atrazine chlorohydrolase activity
D	0019381	biological_process	atrazine catabolic process
D	0046872	molecular_function	metal ion binding
E	0005737	cellular_component	cytoplasm
E	0016787	molecular_function	hydrolase activity
E	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
E	0018788	molecular_function	atrazine chlorohydrolase activity
E	0019381	biological_process	atrazine catabolic process
E	0046872	molecular_function	metal ion binding
F	0005737	cellular_component	cytoplasm
F	0016787	molecular_function	hydrolase activity
F	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
F	0018788	molecular_function	atrazine chlorohydrolase activity
F	0019381	biological_process	atrazine catabolic process
F	0046872	molecular_function	metal ion binding
G	0005737	cellular_component	cytoplasm
G	0016787	molecular_function	hydrolase activity
G	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
G	0018788	molecular_function	atrazine chlorohydrolase activity
G	0019381	biological_process	atrazine catabolic process
G	0046872	molecular_function	metal ion binding
H	0005737	cellular_component	cytoplasm
H	0016787	molecular_function	hydrolase activity
H	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
H	0018788	molecular_function	atrazine chlorohydrolase activity
H	0019381	biological_process	atrazine catabolic process
H	0046872	molecular_function	metal ion binding
I	0005737	cellular_component	cytoplasm
I	0016787	molecular_function	hydrolase activity
I	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
I	0018788	molecular_function	atrazine chlorohydrolase activity
I	0019381	biological_process	atrazine catabolic process
I	0046872	molecular_function	metal ion binding
J	0005737	cellular_component	cytoplasm
J	0016787	molecular_function	hydrolase activity
J	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
J	0018788	molecular_function	atrazine chlorohydrolase activity
J	0019381	biological_process	atrazine catabolic process
J	0046872	molecular_function	metal ion binding
K	0005737	cellular_component	cytoplasm
K	0016787	molecular_function	hydrolase activity
K	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
K	0018788	molecular_function	atrazine chlorohydrolase activity
K	0019381	biological_process	atrazine catabolic process
K	0046872	molecular_function	metal ion binding
L	0005737	cellular_component	cytoplasm
L	0016787	molecular_function	hydrolase activity
L	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
L	0018788	molecular_function	atrazine chlorohydrolase activity
L	0019381	biological_process	atrazine catabolic process
L	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 481

Chain	Residue
A	HIS66
A	HIS68
A	HIS243
A	HIS276
A	ASP327

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE B 481

Chain	Residue
B	ASP327
B	HIS66
B	HIS68
B	HIS243
B	HIS276

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE C 481

Chain	Residue
C	HIS66
C	HIS68
C	HIS243
C	HIS276
C	ASP327

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE D 481

Chain	Residue
D	HIS66
D	HIS68
D	HIS243
D	HIS276
D	ASP327

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE E 481

Chain	Residue
E	HIS66
E	HIS68
E	HIS243
E	HIS276
E	ASP327

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE F 481

Chain	Residue
F	HIS66
F	HIS68
F	HIS243
F	HIS276
F	ASP327

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE G 481

Chain	Residue
G	HIS66
G	HIS68
G	HIS243
G	HIS276
G	ASP327

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE H 481

Chain	Residue
H	HIS66
H	HIS68
H	HIS243
H	HIS276
H	ASP327

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE I 481

Chain	Residue
I	HIS66
I	HIS68
I	HIS243
I	HIS276
I	ASP327

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE J 481

Chain	Residue
J	HIS66
J	HIS68
J	HIS243
J	HIS276
J	ASP327

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE K 481

Chain	Residue
K	HIS66
K	HIS68
K	HIS243
K	HIS276
K	ASP327

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE L 481

Chain	Residue
L	HIS66
L	HIS68
L	HIS243
L	HIS276
L	ASP327

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO L 1475

Chain	Residue
L	ARG19

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO F 1475

Chain	Residue
F	ARG19
F	LEU36

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 1475

Chain	Residue
C	ARG282
C	GLU314
C	ARG318
F	ARG282
F	GLU314
F	ARG318

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO J 1475

Chain	Residue
J	GLU260
J	LYS283

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO H 1475

Chain	Residue
H	GLU260
H	LYS283
L	HOH2008

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO G 1475

Chain	Residue
G	GLU260
G	LYS283

site_id	CC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO E 1475

Chain	Residue
E	GLU260
E	LYS283

site_id	CC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 1475

Chain	Residue
A	LYS283

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1476

Chain	Residue
A	ARG282
A	GLU314
A	ARG318
D	ARG282
D	GLU314
D	ARG318

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO L 1476

Chain	Residue
I	ARG282
I	GLU314
I	ARG318
L	ARG282
L	GLU314
L	ARG318

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO J 1476

Chain	Residue
G	ARG282
G	GLU314
G	ARG318
J	ARG282
J	GLU314
J	ARG318

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 1475

Chain	Residue
B	ARG318
E	ARG282
E	GLU314
E	ARG318
B	ARG282
B	GLU314

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL H 1476

Chain	Residue
H	ARG318
K	ARG318

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG B 1476

Chain	Residue
B	GLU260
B	LYS283
B	ARG290
E	ASP356
F	ARG174

site_id	CC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG C 1476

Chain	Residue
C	GLU260
C	LYS283
C	HOH2007
E	TYR167
E	ARG174

site_id	DC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG I 1475

Chain	Residue
I	GLU260
I	LYS283
I	LEU287
I	ARG290
K	ARG174
L	ASP356

site_id	DC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG F 1476

Chain	Residue
C	HOH2011
D	GLN83
D	ARG174
F	GLU260
F	LYS283

site_id	DC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG K 1475

Chain	Residue
G	ARG174
H	ASP356
K	GLU260
K	GLU263
K	LYS283
K	ARG290

site_id	DC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG D 1475

Chain	Residue
A	ASP356
B	ARG174
D	LYS283
D	LEU287
D	ARG290

site_id	DC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG L 1477

Chain	Residue
I	ASP356
J	ARG174
L	GLU260
L	LYS283
L	ARG290

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	BINDING: BINDING => ECO:0000269\|PubMed:25760618, ECO:0007744\|PDB:4V1Y

Chain	Residue	Details
A	HIS66
C	HIS68
C	HIS276
C	ASP327
D	HIS66
D	HIS68
D	HIS276
D	ASP327
E	HIS66
E	HIS68
E	HIS276
A	HIS68
E	ASP327
F	HIS66
F	HIS68
F	HIS276
F	ASP327
G	HIS66
G	HIS68
G	HIS276
G	ASP327
H	HIS66
A	HIS276
H	HIS68
H	HIS276
H	ASP327
I	HIS66
I	HIS68
I	HIS276
I	ASP327
J	HIS66
J	HIS68
J	HIS276
A	ASP327
J	ASP327
K	HIS66
K	HIS68
K	HIS276
K	ASP327
L	HIS66
L	HIS68
L	HIS276
L	ASP327
B	HIS66
B	HIS68
B	HIS276
B	ASP327
C	HIS66

site_id	SWS_FT_FI2
Number of Residues	36
Details	SITE: Major determinant of atrazine specificity => ECO:0000305\|PubMed:22768133

Chain	Residue	Details
A	PHE84
D	PHE84
D	ASN328
D	SER331
E	PHE84
E	ASN328
E	SER331
F	PHE84
F	ASN328
F	SER331
G	PHE84
A	ASN328
G	ASN328
G	SER331
H	PHE84
H	ASN328
H	SER331
I	PHE84
I	ASN328
I	SER331
J	PHE84
J	ASN328
A	SER331
J	SER331
K	PHE84
K	ASN328
K	SER331
L	PHE84
L	ASN328
L	SER331
B	PHE84
B	ASN328
B	SER331
C	PHE84
C	ASN328
C	SER331

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