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	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	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	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	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	4
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	SER43
B	SER43
C	SER43
D	SER43

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: axial binding residue => ECO:0000255\|PROSITE-ProRule:PRU00297, ECO:0000269\|PubMed:7703247

Chain	Residue	Details
A	THR164
B	THR164
C	THR164
D	THR164

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:7703247, ECO:0007744\|PDB:1APX

Chain	Residue	Details
D	SER181
D	PRO183
D	PHE186
D	ASN188
A	ILE165
A	SER181
A	PRO183
A	PHE186
A	ASN188
B	ILE165
B	SER181
B	PRO183
B	PHE186
B	ASN188
C	ILE165
C	SER181
C	PRO183
C	PHE186
C	ASN188
D	ILE165

site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Transition state stabilizer

Chain	Residue	Details
A	LEU39
B	LEU39
C	LEU39
D	LEU39

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 399

Chain	Residue	Details
A	LEU39	transition state stabiliser
A	SER43	proton shuttle (general acid/base)
A	THR164	activator, metal ligand
A	THR180	radical stabiliser
A	LYS209	activator

site_id	MCSA2
Number of Residues	5
Details	M-CSA 399

Chain	Residue	Details
B	LEU39	transition state stabiliser
B	SER43	proton shuttle (general acid/base)
B	THR164	activator, metal ligand
B	THR180	radical stabiliser
B	LYS209	activator

site_id	MCSA3
Number of Residues	5
Details	M-CSA 399

Chain	Residue	Details
C	LEU39	transition state stabiliser
C	SER43	proton shuttle (general acid/base)
C	THR164	activator, metal ligand
C	THR180	radical stabiliser
C	LYS209	activator

site_id	MCSA4
Number of Residues	5
Details	M-CSA 399

Chain	Residue	Details
D	LEU39	transition state stabiliser
D	SER43	proton shuttle (general acid/base)
D	THR164	activator, metal ligand
D	THR180	radical stabiliser
D	LYS209	activator

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