Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1ZZ9

Crystal Structure of FeII HppE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0008198	molecular_function	ferrous iron binding
A	0016717	molecular_function	oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
A	0017000	biological_process	antibiotic biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0051213	molecular_function	dioxygenase activity
A	0051289	biological_process	protein homotetramerization
A	0055114	biological_process	obsolete oxidation-reduction process
A	1901766	biological_process	phosphinothricin biosynthetic process
B	0003677	molecular_function	DNA binding
B	0008198	molecular_function	ferrous iron binding
B	0016717	molecular_function	oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
B	0017000	biological_process	antibiotic biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0051213	molecular_function	dioxygenase activity
B	0051289	biological_process	protein homotetramerization
B	0055114	biological_process	obsolete oxidation-reduction process
B	1901766	biological_process	phosphinothricin biosynthetic process
C	0003677	molecular_function	DNA binding
C	0008198	molecular_function	ferrous iron binding
C	0016717	molecular_function	oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
C	0017000	biological_process	antibiotic biosynthetic process
C	0046872	molecular_function	metal ion binding
C	0051213	molecular_function	dioxygenase activity
C	0051289	biological_process	protein homotetramerization
C	0055114	biological_process	obsolete oxidation-reduction process
C	1901766	biological_process	phosphinothricin biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE2 A 199

Chain	Residue
A	HIS138
A	GLU142
A	HIS180
A	HOH203
A	HOH232
A	HOH233

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 B 199

Chain	Residue
B	HOH204
B	HOH205
B	HIS138
B	GLU142
B	HIS180

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 C 199

Chain	Residue
C	HIS138
C	GLU142
C	HIS180
C	HOH243
C	HOH244

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 200

Chain	Residue
B	ARG90
B	VAL121
B	LYS192

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 200

Chain	Residue
A	ARG90
A	PHE145
A	LYS192
A	HOH230
A	HOH231
B	HOH221

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 200

Chain	Residue
C	ARG90
C	PHE145
C	HOH241
C	HOH242

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	57
Details	DNA_BIND: H-T-H motif => ECO:0000255\|PROSITE-ProRule:PRU00257

Chain	Residue	Details
A	HIS26-ASN45
B	HIS26-ASN45
C	HIS26-ASN45

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:16186494, ECO:0000269\|PubMed:21682308, ECO:0007744\|PDB:2BNN, ECO:0007744\|PDB:3SCH, ECO:0007744\|PDB:4J1W, ECO:0007744\|PDB:4J1X

Chain	Residue	Details
A	LYS23
B	LYS23
C	LYS23

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:16015285, ECO:0000269\|PubMed:16186494, ECO:0000269\|PubMed:21682308, ECO:0007744\|PDB:1ZZ8, ECO:0007744\|PDB:2BNN, ECO:0007744\|PDB:3SCG, ECO:0007744\|PDB:3SCH, ECO:0007744\|PDB:4J1W, ECO:0007744\|PDB:4J1X

Chain	Residue	Details
A	ARG97
B	ARG97
C	ARG97

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:16015285, ECO:0000269\|PubMed:16186494, ECO:0000269\|PubMed:21682308, ECO:0007744\|PDB:1ZZ8, ECO:0007744\|PDB:1ZZB, ECO:0007744\|PDB:2BNN, ECO:0007744\|PDB:3SCF, ECO:0007744\|PDB:3SCG, ECO:0007744\|PDB:3SCH, ECO:0007744\|PDB:4J1W, ECO:0007744\|PDB:4J1X

Chain	Residue	Details
A	TYR105
B	TYR105
C	TYR105

site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:16015285, ECO:0000269\|PubMed:16186494, ECO:0000269\|PubMed:21682308, ECO:0007744\|PDB:1ZZ7, ECO:0007744\|PDB:1ZZ8, ECO:0007744\|PDB:1ZZB, ECO:0007744\|PDB:2BNN, ECO:0007744\|PDB:3SCF, ECO:0007744\|PDB:3SCG, ECO:0007744\|PDB:3SCH, ECO:0007744\|PDB:4J1W, ECO:0007744\|PDB:4J1X

Chain	Residue	Details
A	ASN135
B	ASN135
C	ASN135

site_id	SWS_FT_FI6
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:16015285, ECO:0000269\|PubMed:16186494, ECO:0000269\|PubMed:21682308, ECO:0007744\|PDB:1ZZ7, ECO:0007744\|PDB:1ZZ8, ECO:0007744\|PDB:1ZZ9, ECO:0007744\|PDB:2BNM, ECO:0007744\|PDB:2BNN, ECO:0007744\|PDB:2BNO, ECO:0007744\|PDB:3SCF, ECO:0007744\|PDB:3SCG, ECO:0007744\|PDB:4J1W, ECO:0007744\|PDB:4J1X

Chain	Residue	Details
A	HIS138
A	HIS180
B	HIS138
B	HIS180
C	HIS138
C	HIS180

site_id	SWS_FT_FI7
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:16015285, ECO:0000269\|PubMed:16186494, ECO:0000269\|PubMed:21682308, ECO:0007744\|PDB:1ZZ7, ECO:0007744\|PDB:1ZZ8, ECO:0007744\|PDB:1ZZB, ECO:0007744\|PDB:2BNN, ECO:0007744\|PDB:3SCF, ECO:0007744\|PDB:3SCG, ECO:0007744\|PDB:3SCH, ECO:0007744\|PDB:4J1W

Chain	Residue	Details
A	GLU142
B	GLU142
C	GLU142

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