Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6KMM

Crystal Structure of HEPES bound Dye Decolorizing peroxidase from Bacillus subtilis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004325	molecular_function	ferrochelatase activity
A	0004601	molecular_function	peroxidase activity
A	0005576	cellular_component	extracellular region
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0016829	molecular_function	lyase activity
A	0020037	molecular_function	heme binding
A	0033212	biological_process	iron import into cell
A	0046872	molecular_function	metal ion binding
A	0098869	biological_process	cellular oxidant detoxification
B	0004325	molecular_function	ferrochelatase activity
B	0004601	molecular_function	peroxidase activity
B	0005576	cellular_component	extracellular region
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0016829	molecular_function	lyase activity
B	0020037	molecular_function	heme binding
B	0033212	biological_process	iron import into cell
B	0046872	molecular_function	metal ion binding
B	0098869	biological_process	cellular oxidant detoxification
C	0004325	molecular_function	ferrochelatase activity
C	0004601	molecular_function	peroxidase activity
C	0005576	cellular_component	extracellular region
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0016829	molecular_function	lyase activity
C	0020037	molecular_function	heme binding
C	0033212	biological_process	iron import into cell
C	0046872	molecular_function	metal ion binding
C	0098869	biological_process	cellular oxidant detoxification
D	0004325	molecular_function	ferrochelatase activity
D	0004601	molecular_function	peroxidase activity
D	0005576	cellular_component	extracellular region
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0016829	molecular_function	lyase activity
D	0020037	molecular_function	heme binding
D	0033212	biological_process	iron import into cell
D	0046872	molecular_function	metal ion binding
D	0098869	biological_process	cellular oxidant detoxification
E	0004325	molecular_function	ferrochelatase activity
E	0004601	molecular_function	peroxidase activity
E	0005576	cellular_component	extracellular region
E	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0016829	molecular_function	lyase activity
E	0020037	molecular_function	heme binding
E	0033212	biological_process	iron import into cell
E	0046872	molecular_function	metal ion binding
E	0098869	biological_process	cellular oxidant detoxification
F	0004325	molecular_function	ferrochelatase activity
F	0004601	molecular_function	peroxidase activity
F	0005576	cellular_component	extracellular region
F	0005829	cellular_component	cytosol
F	0005886	cellular_component	plasma membrane
F	0016829	molecular_function	lyase activity
F	0020037	molecular_function	heme binding
F	0033212	biological_process	iron import into cell
F	0046872	molecular_function	metal ion binding
F	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	binding site for residue HEM A 401

Chain	Residue
A	ASN181
A	HIS273
A	ALA277
A	LYS278
A	ARG286
A	LEU306
A	PHE308
A	PHE319
A	MET322
A	LEU326
A	LEU332
A	PHE185
A	OXY402
A	HOH537
A	HOH579
A	HOH617
A	LYS186
A	ASP187
A	GLY188
A	THR189
A	GLY190
A	ILE225
A	PHE244

site_id	AC2
Number of Residues	3
Details	binding site for residue OXY A 402

Chain	Residue
A	ASP187
A	ARG286
A	HEM401

site_id	AC3
Number of Residues	5
Details	binding site for residue EPE A 403

Chain	Residue
A	THR189
A	GLN192
A	THR260
A	LYS278
A	HOH537

site_id	AC4
Number of Residues	4
Details	binding site for residue GOL A 404

Chain	Residue
A	HIS20
A	THR22
A	ASP140
A	HOH658

site_id	AC5
Number of Residues	3
Details	binding site for residue GOL A 405

Chain	Residue
A	ARG44
A	SER48
A	GLU354

site_id	AC6
Number of Residues	5
Details	binding site for residue GOL A 406

Chain	Residue
A	HOH650
A	HOH664
E	TYR301
E	MET302
E	HOH531

site_id	AC7
Number of Residues	23
Details	binding site for residue HEM B 401

Chain	Residue
B	ASN181
B	PHE185
B	LYS186
B	ASP187
B	GLY188
B	THR189
B	GLY190
B	ILE225
B	PHE244
B	HIS273
B	ALA277
B	LYS278
B	ARG286
B	LEU306
B	PHE308
B	MET322
B	LEU326
B	LEU332
B	OXY402
B	HOH529
B	HOH533
B	HOH544
B	HOH618

site_id	AC8
Number of Residues	3
Details	binding site for residue OXY B 402

Chain	Residue
B	ASP187
B	ARG286
B	HEM401

site_id	AC9
Number of Residues	6
Details	binding site for residue NA B 403

Chain	Residue
B	THR292
B	GLU293
B	GLY294
B	MET302
C	TYR25
C	LYS167

site_id	AD1
Number of Residues	6
Details	binding site for residue MPD B 404

Chain	Residue
B	MET302
C	LEU153
C	ASN154
C	VAL162
C	HOH551
C	HOH630

site_id	AD2
Number of Residues	23
Details	binding site for residue HEM C 401

Chain	Residue
C	LEU332
C	OXY402
C	HOH523
C	HOH596
C	HOH693
C	PHE185
C	LYS186
C	GLY188
C	THR189
C	GLY190
C	ILE225
C	MET227
C	PHE244
C	ARG246
C	HIS273
C	VAL274
C	ALA277
C	LYS278
C	ARG286
C	PHE308
C	PHE319
C	MET322
C	LEU326

site_id	AD3
Number of Residues	3
Details	binding site for residue OXY C 402

Chain	Residue
C	ASP187
C	ARG286
C	HEM401

site_id	AD4
Number of Residues	7
Details	binding site for residue EPE C 403

Chain	Residue
C	ARG234
C	SER235
C	GLU334
C	TYR335
C	HOH516
C	HOH776
E	SER270

site_id	AD5
Number of Residues	2
Details	binding site for residue GOL C 404

Chain	Residue
C	ARG44
C	SER48

site_id	AD6
Number of Residues	2
Details	binding site for residue PO4 C 405

Chain	Residue
C	ASP38
C	GLY158

site_id	AD7
Number of Residues	4
Details	binding site for residue MPD C 406

Chain	Residue
B	ASN154
B	VAL157
C	TYR301
C	MET302

site_id	AD8
Number of Residues	2
Details	binding site for residue CL C 407

Chain	Residue
A	SER198
C	SER198

site_id	AD9
Number of Residues	22
Details	binding site for residue HEM D 401

Chain	Residue
D	ASN181
D	PHE185
D	LYS186
D	ASP187
D	GLY188
D	THR189
D	GLY190
D	ILE225
D	PHE244
D	HIS273
D	VAL274
D	LYS278
D	ARG286
D	PHE308
D	PHE319
D	MET322
D	LEU326
D	LEU332
D	OXY402
D	HOH521
D	HOH543
D	HOH695

site_id	AE1
Number of Residues	3
Details	binding site for residue OXY D 402

Chain	Residue
D	ASP187
D	ARG286
D	HEM401

site_id	AE2
Number of Residues	6
Details	binding site for residue EPE D 403

Chain	Residue
B	HOH545
D	ARG234
D	SER235
D	ASP239
D	GLU334
D	TYR335

site_id	AE3
Number of Residues	10
Details	binding site for residue EPE D 404

Chain	Residue
D	THR189
D	ASN191
D	GLU259
D	THR260
D	PRO262
D	VAL263
D	LYS278
D	HOH505
D	HOH521
D	HOH784

site_id	AE4
Number of Residues	7
Details	binding site for residue MPD D 405

Chain	Residue
D	TYR301
D	MET302
F	LEU153
F	ASN154
F	VAL157
F	VAL162
F	HOH592

site_id	AE5
Number of Residues	22
Details	binding site for residue HEM E 401

Chain	Residue
E	PHE185
E	LYS186
E	ASP187
E	GLY188
E	THR189
E	GLY190
E	ILE225
E	PHE244
E	HIS273
E	VAL274
E	ALA277
E	LYS278
E	ARG286
E	LEU306
E	PHE308
E	PHE319
E	MET322
E	LEU332
E	OXY402
E	HOH542
E	HOH585
E	HOH606

site_id	AE6
Number of Residues	3
Details	binding site for residue OXY E 402

Chain	Residue
E	ASP187
E	ARG286
E	HEM401

site_id	AE7
Number of Residues	1
Details	binding site for residue GOL E 403

Chain	Residue
E	HOH502

site_id	AE8
Number of Residues	6
Details	binding site for residue GOL E 404

Chain	Residue
E	ASP330
E	ASN333
E	THR336
E	THR338
E	HOH665
E	HOH699

site_id	AE9
Number of Residues	24
Details	binding site for residue HEM F 401

Chain	Residue
F	ASN181
F	PHE185
F	LYS186
F	ASP187
F	GLY188
F	THR189
F	GLY190
F	MET227
F	PHE244
F	HIS273
F	VAL274
F	LYS278
F	ARG286
F	LEU306
F	PHE308
F	PHE319
F	MET322
F	LEU323
F	LEU326
F	LEU332
F	OXY402
F	HOH519
F	HOH589
F	HOH632

site_id	AF1
Number of Residues	3
Details	binding site for residue OXY F 402

Chain	Residue
F	ASP187
F	ARG286
F	HEM401

site_id	AF2
Number of Residues	7
Details	binding site for residue EPE F 403

Chain	Residue
A	SER270
F	ARG234
F	SER235
F	ASP239
F	GLU334
F	TYR335
F	HOH687

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:32971035, ECO:0000269\|PubMed:36345957, ECO:0007744\|PDB:6KMN, ECO:0007744\|PDB:7E5Q

Chain	Residue	Details
A	GLY188
B	GLY188
C	GLY188
D	GLY188
E	GLY188
F	GLY188

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: proximal binding residue => ECO:0000269\|PubMed:32971035, ECO:0000269\|PubMed:36345957, ECO:0007744\|PDB:6KMM, ECO:0007744\|PDB:6KMN, ECO:0007744\|PDB:7E5Q

Chain	Residue	Details
A	HIS273
B	HIS273
C	HIS273
D	HIS273
E	HIS273
F	HIS273

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:32971035, ECO:0000269\|PubMed:36345957, ECO:0007744\|PDB:6KMM, ECO:0007744\|PDB:6KMN, ECO:0007744\|PDB:7E5Q

Chain	Residue	Details
A	ARG286
B	ARG286
C	ARG286
D	ARG286
E	ARG286
F	ARG286

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