Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6RJR

Crystal structure of a Fungal Catalase at 1.9 Angstrom

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000302	biological_process	response to reactive oxygen species
A	0004096	molecular_function	catalase activity
A	0004601	molecular_function	peroxidase activity
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005777	cellular_component	peroxisome
A	0006979	biological_process	response to oxidative stress
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
A	0042542	biological_process	response to hydrogen peroxide
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0046872	molecular_function	metal ion binding
A	0098869	biological_process	cellular oxidant detoxification
B	0000166	molecular_function	nucleotide binding
B	0000302	biological_process	response to reactive oxygen species
B	0004096	molecular_function	catalase activity
B	0004601	molecular_function	peroxidase activity
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005777	cellular_component	peroxisome
B	0006979	biological_process	response to oxidative stress
B	0016491	molecular_function	oxidoreductase activity
B	0020037	molecular_function	heme binding
B	0042542	biological_process	response to hydrogen peroxide
B	0042744	biological_process	hydrogen peroxide catabolic process
B	0046872	molecular_function	metal ion binding
B	0098869	biological_process	cellular oxidant detoxification
C	0000166	molecular_function	nucleotide binding
C	0000302	biological_process	response to reactive oxygen species
C	0004096	molecular_function	catalase activity
C	0004601	molecular_function	peroxidase activity
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005777	cellular_component	peroxisome
C	0006979	biological_process	response to oxidative stress
C	0016491	molecular_function	oxidoreductase activity
C	0020037	molecular_function	heme binding
C	0042542	biological_process	response to hydrogen peroxide
C	0042744	biological_process	hydrogen peroxide catabolic process
C	0046872	molecular_function	metal ion binding
C	0098869	biological_process	cellular oxidant detoxification
D	0000166	molecular_function	nucleotide binding
D	0000302	biological_process	response to reactive oxygen species
D	0004096	molecular_function	catalase activity
D	0004601	molecular_function	peroxidase activity
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005777	cellular_component	peroxisome
D	0006979	biological_process	response to oxidative stress
D	0016491	molecular_function	oxidoreductase activity
D	0020037	molecular_function	heme binding
D	0042542	biological_process	response to hydrogen peroxide
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	24
Details	binding site for residue HEM A 601

Chain	Residue
A	ARG61
A	SER207
A	HIS209
A	LEU290
A	PHE325
A	VAL341
A	ARG345
A	SER348
A	TYR349
A	ALA352
A	HIS353
A	ASN62
A	ARG356
A	HOH723
A	HOH759
A	HOH765
B	ASN54
A	HIS64
A	ARG101
A	GLY120
A	VAL135
A	ASN136
A	ASN137
A	PHE150

site_id	AC2
Number of Residues	24
Details	binding site for residue NDP A 602

Chain	Residue
A	HIS185
A	SER192
A	ARG194
A	ASN204
A	HIS226
A	LYS228
A	VAL293
A	TRP294
A	HIS296
A	GLN439
A	LEU443
A	VAL447
A	GLN451
A	HOH725
A	HOH727
A	HOH738
A	HOH741
A	HOH744
A	HOH748
A	HOH789
A	HOH807
A	HOH812
A	HOH825
A	HOH891

site_id	AC3
Number of Residues	4
Details	binding site for residue GOL A 603

Chain	Residue
A	ARG116
A	ASN238
A	THR242
A	ALA245

site_id	AC4
Number of Residues	4
Details	binding site for residue GOL A 604

Chain	Residue
A	LYS494
A	HOH732
A	HOH813
A	HOH880

site_id	AC5
Number of Residues	3
Details	binding site for residue GOL A 605

Chain	Residue
A	PRO452
A	HOH935
D	GLU490

site_id	AC6
Number of Residues	8
Details	binding site for residue GOL A 606

Chain	Residue
A	GLY110
A	ALA112
A	ALA245
A	PRO249
A	HOH972
B	SER111
B	ALA112
B	ALA245

site_id	AC7
Number of Residues	8
Details	binding site for residue GOL A 607

Chain	Residue
A	ARG145
A	PHE285
A	SER286
A	ASP289
A	SER431
A	ILE435
A	ASP436
A	HOH701

site_id	AC8
Number of Residues	5
Details	binding site for residue GOL A 608

Chain	Residue
A	PRO284
A	PRO295
A	VAL438
A	GLN439
A	ASP442

site_id	AC9
Number of Residues	5
Details	binding site for residue K A 609

Chain	Residue
A	PRO140
A	GLY208
A	LYS292
A	HOH819
A	HOH892

site_id	AD1
Number of Residues	23
Details	binding site for residue HEM B 601

Chain	Residue
B	ARG345
B	SER348
B	TYR349
B	ALA352
B	HIS353
B	ARG356
B	HOH729
B	HOH741
B	HOH812
A	ASN54
B	ARG61
B	ASN62
B	HIS64
B	ARG101
B	GLY120
B	VAL135
B	ASN136
B	ASN137
B	PHE150
B	HIS209
B	LEU290
B	PHE325
B	VAL341

site_id	AD2
Number of Residues	20
Details	binding site for residue NDP B 602

Chain	Residue
B	HIS185
B	SER192
B	ARG194
B	ASN204
B	HIS226
B	LYS228
B	ILE233
B	VAL293
B	TRP294
B	HIS296
B	GLN439
B	LEU443
B	VAL447
B	LEU448
B	GLN451
B	HOH710
B	HOH795
B	HOH843
B	HOH850
B	HOH890

site_id	AD3
Number of Residues	3
Details	binding site for residue GOL B 603

Chain	Residue
B	THR114
B	ARG116
B	ASN238

site_id	AD4
Number of Residues	5
Details	binding site for residue K B 604

Chain	Residue
B	PRO140
B	GLY208
B	LYS292
B	HOH804
B	HOH859

site_id	AD5
Number of Residues	4
Details	binding site for residue CL B 605

Chain	Residue
A	HOH768
B	ARG55
C	ARG55
D	HOH774

site_id	AD6
Number of Residues	20
Details	binding site for residue HEM C 601

Chain	Residue
C	ARG61
C	ASN62
C	HIS64
C	ARG101
C	GLY120
C	ASN136
C	ASN137
C	PHE150
C	LEU290
C	PHE325
C	VAL341
C	ARG345
C	SER348
C	TYR349
C	HIS353
C	ARG356
C	HOH715
C	HOH725
C	HOH811
D	ASN54

site_id	AD7
Number of Residues	24
Details	binding site for residue NDP C 602

Chain	Residue
C	PRO140
C	HIS185
C	SER192
C	ARG194
C	ASN204
C	HIS226
C	LYS228
C	ILE233
C	TRP294
C	PRO295
C	HIS296
C	GLN439
C	LEU443
C	VAL447
C	LEU448
C	GLN451
C	HOH707
C	HOH717
C	HOH732
C	HOH779
C	HOH802
C	HOH808
C	HOH817
C	HOH917

site_id	AD8
Number of Residues	4
Details	binding site for residue GOL C 603

Chain	Residue
C	THR114
C	ARG116
C	ASN238
C	THR242

site_id	AD9
Number of Residues	7
Details	binding site for residue GOL C 604

Chain	Residue
C	GLY110
C	ALA112
C	ALA245
C	PRO249
D	ALA112
D	ALA245
D	PRO249

site_id	AE1
Number of Residues	7
Details	binding site for residue K C 605

Chain	Residue
C	PRO140
C	GLY208
C	GLN224
C	LEU290
C	LYS292
C	HOH785
C	HOH875

site_id	AE2
Number of Residues	3
Details	binding site for residue CL D 601

Chain	Residue
A	ARG55
B	HOH776
D	ARG55

site_id	AE3
Number of Residues	25
Details	binding site for residue HEM D 602

Chain	Residue
C	ASN54
D	ARG61
D	ASN62
D	HIS64
D	ARG101
D	GLY120
D	VAL135
D	ASN136
D	ASN137
D	PHE150
D	HIS209
D	LEU290
D	PHE325
D	VAL341
D	ARG345
D	SER348
D	TYR349
D	ALA352
D	HIS353
D	ARG356
D	HOH715
D	HOH747
D	HOH748
D	HOH786
D	HOH791

site_id	AE4
Number of Residues	23
Details	binding site for residue NDP D 603

Chain	Residue
D	PRO140
D	HIS185
D	SER192
D	ARG194
D	ASN204
D	HIS226
D	LYS228
D	VAL293
D	TRP294
D	PRO295
D	HIS296
D	GLN439
D	LEU443
D	VAL447
D	LEU448
D	GLN451
D	HOH714
D	HOH718
D	HOH722
D	HOH756
D	HOH762
D	HOH783
D	HOH900

site_id	AE5
Number of Residues	5
Details	binding site for residue GOL D 604

Chain	Residue
D	ALA482
D	ARG483
D	VAL484
D	ASP485
D	ARG486

site_id	AE6
Number of Residues	6
Details	binding site for residue GOL D 605

Chain	Residue
D	THR114
D	ALA115
D	ARG116
D	ASN238
D	ALA241
D	THR242

site_id	AE7
Number of Residues	6
Details	binding site for residue K D 606

Chain	Residue
D	PRO140
D	GLY208
D	LEU290
D	LYS292
D	HOH876
D	HOH889

Functional Information from PROSITE/UniProt

site_id	PS00437
Number of Residues	9
Details	CATALASE_1 Catalase proximal heme-ligand signature. RLFSYpDAH

Chain	Residue	Details
A	ARG345-HIS353

site_id	PS00438
Number of Residues	17
Details	CATALASE_2 Catalase proximal active site signature. FnReripERnpHahGSG

Chain	Residue	Details
A	PHE53-GLY69

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