Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1APX

CRYSTAL STRUCTURE OF RECOMBINANT ASCORBATE PEROXIDASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000302	biological_process	response to reactive oxygen species
A	0004601	molecular_function	peroxidase activity
A	0005737	cellular_component	cytoplasm
A	0006979	biological_process	response to oxidative stress
A	0009507	cellular_component	chloroplast
A	0016491	molecular_function	oxidoreductase activity
A	0016688	molecular_function	L-ascorbate peroxidase activity
A	0020037	molecular_function	heme binding
A	0034599	biological_process	cellular response to oxidative stress
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0046872	molecular_function	metal ion binding
A	0098869	biological_process	cellular oxidant detoxification
B	0000302	biological_process	response to reactive oxygen species
B	0004601	molecular_function	peroxidase activity
B	0005737	cellular_component	cytoplasm
B	0006979	biological_process	response to oxidative stress
B	0009507	cellular_component	chloroplast
B	0016491	molecular_function	oxidoreductase activity
B	0016688	molecular_function	L-ascorbate peroxidase activity
B	0020037	molecular_function	heme binding
B	0034599	biological_process	cellular response to oxidative stress
B	0042744	biological_process	hydrogen peroxide catabolic process
B	0046872	molecular_function	metal ion binding
B	0098869	biological_process	cellular oxidant detoxification
C	0000302	biological_process	response to reactive oxygen species
C	0004601	molecular_function	peroxidase activity
C	0005737	cellular_component	cytoplasm
C	0006979	biological_process	response to oxidative stress
C	0009507	cellular_component	chloroplast
C	0016491	molecular_function	oxidoreductase activity
C	0016688	molecular_function	L-ascorbate peroxidase activity
C	0020037	molecular_function	heme binding
C	0034599	biological_process	cellular response to oxidative stress
C	0042744	biological_process	hydrogen peroxide catabolic process
C	0046872	molecular_function	metal ion binding
C	0098869	biological_process	cellular oxidant detoxification
D	0000302	biological_process	response to reactive oxygen species
D	0004601	molecular_function	peroxidase activity
D	0005737	cellular_component	cytoplasm
D	0006979	biological_process	response to oxidative stress
D	0009507	cellular_component	chloroplast
D	0016491	molecular_function	oxidoreductase activity
D	0016688	molecular_function	L-ascorbate peroxidase activity
D	0020037	molecular_function	heme binding
D	0034599	biological_process	cellular response to oxidative stress
D	0042744	biological_process	hydrogen peroxide catabolic process
D	0046872	molecular_function	metal ion binding
D	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 252

Chain	Residue
A	THR164
A	THR180
A	ASN182
A	ILE185
A	ASP187

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K B 252

Chain	Residue
B	THR164
B	THR180
B	ASN182
B	ILE185
B	ASP187

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K C 252

Chain	Residue
C	THR164
C	THR180
C	ASN182
C	ILE185
C	ASP187

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K D 252

Chain	Residue
D	THR164
D	THR180
D	ASN182
D	ILE185
D	ASP187

site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM A 251

Chain	Residue
A	PRO34
A	TRP41
A	PRO132
A	ALA134
A	PHE145
A	LEU159
A	HIS163
A	ILE165
A	GLY166
A	ALA167
A	ALA168
A	HIS169
A	ARG172
A	SER173
A	TRP179
A	TYR235
A	HOH294
A	HOH295
A	HOH322
A	HOH716

site_id	AC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM B 251

Chain	Residue
B	PRO34
B	TRP41
B	PRO132
B	ALA134
B	LEU141
B	PHE145
B	LEU159
B	HIS163
B	ILE165
B	GLY166
B	ALA167
B	ALA168
B	HIS169
B	ARG172
B	SER173
B	TRP179
B	TYR235
B	HOH266
B	HOH280
B	HOH364
B	HOH855

site_id	AC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM C 251

Chain	Residue
C	TYR235
C	HOH268
C	HOH272
C	PRO34
C	TRP41
C	PRO132
C	PHE145
C	LEU159
C	SER160
C	HIS163
C	ILE165
C	GLY166
C	ALA167
C	HIS169
C	ARG172
C	SER173
C	TRP179

site_id	AC8
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM D 251

Chain	Residue
D	PRO34
D	TRP41
D	ALA134
D	PHE145
D	LEU159
D	SER160
D	GLY162
D	HIS163
D	ILE165
D	GLY166
D	ALA167
D	ALA168
D	HIS169
D	ARG172
D	SER173
D	TRP179
D	SER207
D	TYR235
D	HOH434
D	HOH435
D	HOH822

site_id	K1
Number of Residues	6
Details	COORDINATING CARBONYL OXYGEN AND SIDE-CHAIN LIGANDS FOR POTASSIUM ION IN CHAIN A

Chain	Residue
A	K252
A	THR164
A	THR180
A	ASN182
A	ILE185
A	ASP187

site_id	K2
Number of Residues	6
Details	COORDINATING CARBONYL OXYGEN AND SIDE-CHAIN LIGANDS FOR POTASSIUM ION IN CHAIN B

Chain	Residue
B	ASN182
B	ILE185
B	ASP187
B	K252
B	THR164
B	THR180

site_id	K3
Number of Residues	6
Details	COORDINATING CARBONYL OXYGEN AND SIDE-CHAIN LIGANDS FOR POTASSIUM ION IN CHAIN C

Chain	Residue
C	K252
C	THR164
C	THR180
C	ASN182
C	ILE185
C	ASP187

site_id	K4
Number of Residues	6
Details	COORDINATING CARBONYL OXYGEN AND SIDE-CHAIN LIGANDS FOR POTASSIUM ION IN CHAIN D

Chain	Residue
D	K252
D	THR164
D	THR180
D	ASN182
D	ILE185
D	ASP187

Functional Information from PROSITE/UniProt

site_id	PS00435
Number of Residues	11
Details	PEROXIDASE_1 Peroxidases proximal heme-ligand signature. DIVALSGGHTI

Chain	Residue	Details
A	ASP155-ILE165

site_id	PS00436
Number of Residues	12
Details	PEROXIDASE_2 Peroxidases active site signature. APliLRLaWHSA

Chain	Residue	Details
A	ALA33-ALA44

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	96
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	80
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7703247","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7703247","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1APX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 3036202, 2790012, 2169873, 7703247, 7665612, 9406554, 10024453, 10187820

Chain	Residue	Details
A	ARG38
A	HIS42
A	ASN71

site_id	CSA2
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 3036202, 2790012, 2169873, 7703247, 7665612, 9406554, 10024453, 10187820

Chain	Residue	Details
B	ARG38
B	HIS42
B	ASN71

site_id	CSA3
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 3036202, 2790012, 2169873, 7703247, 7665612, 9406554, 10024453, 10187820

Chain	Residue	Details
C	ARG38
C	HIS42
C	ASN71

site_id	CSA4
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 3036202, 2790012, 2169873, 7703247, 7665612, 9406554, 10024453, 10187820

Chain	Residue	Details
D	ARG38
D	HIS42
D	ASN71

site_id	MCSA1
Number of Residues	5
Details	M-CSA 399

Chain	Residue	Details
A	ARG38	transition state stabiliser
A	HIS42	proton shuttle (general acid/base)
A	HIS163	activator, metal ligand
A	TRP179	radical stabiliser
A	ASP208	activator

site_id	MCSA2
Number of Residues	5
Details	M-CSA 399

Chain	Residue	Details
B	ARG38	transition state stabiliser
B	HIS42	proton shuttle (general acid/base)
B	HIS163	activator, metal ligand
B	TRP179	radical stabiliser
B	ASP208	activator

site_id	MCSA3
Number of Residues	5
Details	M-CSA 399

Chain	Residue	Details
C	ARG38	transition state stabiliser
C	HIS42	proton shuttle (general acid/base)
C	HIS163	activator, metal ligand
C	TRP179	radical stabiliser
C	ASP208	activator

site_id	MCSA4
Number of Residues	5
Details	M-CSA 399

Chain	Residue	Details
D	ARG38	transition state stabiliser
D	HIS42	proton shuttle (general acid/base)
D	HIS163	activator, metal ligand
D	TRP179	radical stabiliser
D	ASP208	activator

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