Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6ZIJ

Crystal Structure of Two-Domain Laccase mutant R240H from Streptomyces griseoflavus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0005886	cellular_component	plasma membrane
A	0006826	biological_process	iron ion transport
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0052716	molecular_function	hydroquinone:oxygen oxidoreductase activity
B	0005507	molecular_function	copper ion binding
B	0005886	cellular_component	plasma membrane
B	0006826	biological_process	iron ion transport
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
B	0052716	molecular_function	hydroquinone:oxygen oxidoreductase activity
C	0005507	molecular_function	copper ion binding
C	0005886	cellular_component	plasma membrane
C	0006826	biological_process	iron ion transport
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
C	0052716	molecular_function	hydroquinone:oxygen oxidoreductase activity
D	0005507	molecular_function	copper ion binding
D	0005886	cellular_component	plasma membrane
D	0006826	biological_process	iron ion transport
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
D	0052716	molecular_function	hydroquinone:oxygen oxidoreductase activity
E	0005507	molecular_function	copper ion binding
E	0005886	cellular_component	plasma membrane
E	0006826	biological_process	iron ion transport
E	0016491	molecular_function	oxidoreductase activity
E	0046872	molecular_function	metal ion binding
E	0052716	molecular_function	hydroquinone:oxygen oxidoreductase activity
F	0005507	molecular_function	copper ion binding
F	0005886	cellular_component	plasma membrane
F	0006826	biological_process	iron ion transport
F	0016491	molecular_function	oxidoreductase activity
F	0046872	molecular_function	metal ion binding
F	0052716	molecular_function	hydroquinone:oxygen oxidoreductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue CU A 401

Chain	Residue
A	HIS232
A	CYS289
A	HIS294
A	MET299

site_id	AC2
Number of Residues	5
Details	binding site for residue CU A 402

Chain	Residue
A	HIS237
A	MET286
A	HIS288
A	OXY407
C	HIS159

site_id	AC3
Number of Residues	8
Details	binding site for residue GOL A 403

Chain	Residue
A	GLY152
A	TYR153
A	VAL180
A	ARG181
A	ASP185
A	ARG245
A	THR246
A	HOH516

site_id	AC4
Number of Residues	2
Details	binding site for residue EDO A 404

Chain	Residue
A	ARG50
A	GLU81

site_id	AC5
Number of Residues	4
Details	binding site for residue CU A 405

Chain	Residue
A	HIS105
A	HIS157
A	OXY408
B	HIS290

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

Chain	Residue
A	HIS103
A	OXY408
A	HOH508
B	HIS235
B	HIS237

site_id	AC7
Number of Residues	11
Details	binding site for residue OXY A 407

Chain	Residue
A	HIS235
A	HIS237
A	HIS288
A	HIS290
A	CU402
A	HOH520
C	HIS103
C	HIS157
C	HIS159
C	CU401
C	CU402

site_id	AC8
Number of Residues	11
Details	binding site for residue OXY A 408

Chain	Residue
A	HIS103
A	HIS157
A	HIS159
A	CU405
A	CU406
A	HOH501
B	HIS235
B	HIS237
B	HIS288
B	HIS290
B	CU402

site_id	AC9
Number of Residues	5
Details	binding site for residue MG A 409

Chain	Residue
A	HOH559
A	HOH644
B	HOH558
B	HOH666
C	HOH535

site_id	AD1
Number of Residues	4
Details	binding site for residue CU B 401

Chain	Residue
B	HIS232
B	CYS289
B	HIS294
B	MET299

site_id	AD2
Number of Residues	4
Details	binding site for residue CU B 402

Chain	Residue
A	HIS159
A	OXY408
B	HIS237
B	HIS288

site_id	AD3
Number of Residues	6
Details	binding site for residue EDO B 403

Chain	Residue
B	GLY152
B	TYR153
B	VAL180
B	ARG181
B	ASP185
B	ARG245

site_id	AD4
Number of Residues	5
Details	binding site for residue CU B 404

Chain	Residue
B	HIS103
B	HIS105
B	HIS157
B	OXY405
C	HIS290

site_id	AD5
Number of Residues	11
Details	binding site for residue OXY B 405

Chain	Residue
B	HIS103
B	HIS157
B	HIS159
B	CU404
B	HOH541
C	HIS235
C	HIS237
C	HIS288
C	HIS290
C	CU404
C	CU405

site_id	AD6
Number of Residues	5
Details	binding site for residue CU C 401

Chain	Residue
A	HIS290
A	OXY407
C	HIS105
C	HIS157
C	CU402

site_id	AD7
Number of Residues	6
Details	binding site for residue CU C 402

Chain	Residue
A	HIS235
A	HIS237
A	OXY407
C	HIS103
C	HIS105
C	CU401

site_id	AD8
Number of Residues	4
Details	binding site for residue CU C 403

Chain	Residue
C	MET299
C	HIS232
C	CYS289
C	HIS294

site_id	AD9
Number of Residues	4
Details	binding site for residue CU C 404

Chain	Residue
B	HIS159
B	OXY405
C	HIS237
C	HIS288

site_id	AE1
Number of Residues	4
Details	binding site for residue CU C 405

Chain	Residue
B	HIS103
B	OXY405
C	HIS235
C	HIS237

site_id	AE2
Number of Residues	8
Details	binding site for residue GOL C 406

Chain	Residue
C	GLY152
C	TYR153
C	VAL180
C	ARG181
C	ASP185
C	ARG245
C	THR246
C	HOH513

site_id	AE3
Number of Residues	6
Details	binding site for residue MG C 407

Chain	Residue
A	HOH533
A	HOH625
B	HOH607
B	HOH628
C	HOH560
C	HOH643

site_id	AE4
Number of Residues	4
Details	binding site for residue CU D 401

Chain	Residue
D	HIS232
D	CYS289
D	HIS294
D	MET299

site_id	AE5
Number of Residues	4
Details	binding site for residue CU D 402

Chain	Residue
D	HIS237
D	HIS288
D	OXY405
F	HIS159

site_id	AE6
Number of Residues	4
Details	binding site for residue CU D 403

Chain	Residue
D	HIS235
D	HIS237
D	OXY405
F	HIS103

site_id	AE7
Number of Residues	5
Details	binding site for residue CU D 404

Chain	Residue
D	HIS105
D	HIS157
E	HIS290
E	CU403
E	OXY408

site_id	AE8
Number of Residues	11
Details	binding site for residue OXY D 405

Chain	Residue
D	HIS235
D	HIS237
D	HIS288
D	HIS290
D	CU402
D	CU403
D	HOH511
F	HIS103
F	HIS157
F	HIS159
F	CU401

site_id	AE9
Number of Residues	6
Details	binding site for residue MG D 406

Chain	Residue
D	HOH523
D	HOH619
E	HOH530
E	HOH559
F	HOH582
F	HOH625

site_id	AF1
Number of Residues	4
Details	binding site for residue CU E 401

Chain	Residue
E	HIS232
E	CYS289
E	HIS294
E	MET299

site_id	AF2
Number of Residues	4
Details	binding site for residue CU E 402

Chain	Residue
D	HIS159
E	HIS237
E	HIS288
E	OXY408

site_id	AF3
Number of Residues	6
Details	binding site for residue CU E 403

Chain	Residue
D	HIS103
D	HIS105
D	CU404
E	HIS235
E	HIS237
E	OXY408

site_id	AF4
Number of Residues	4
Details	binding site for residue GOL E 404

Chain	Residue
E	ARG50
E	LEU79
E	ILE80
E	GLU81

site_id	AF5
Number of Residues	4
Details	binding site for residue GOL E 405

Chain	Residue
E	ARG51
E	HIS89
E	THR130
E	HOH512

site_id	AF6
Number of Residues	5
Details	binding site for residue CU E 406

Chain	Residue
E	HIS105
E	HIS157
E	CU407
E	OXY409
F	HIS290

site_id	AF7
Number of Residues	6
Details	binding site for residue CU E 407

Chain	Residue
E	HIS103
E	HIS105
E	CU406
E	OXY409
F	HIS235
F	HIS237

site_id	AF8
Number of Residues	11
Details	binding site for residue OXY E 408

Chain	Residue
D	HIS103
D	HIS157
D	HIS159
D	CU404
E	HIS235
E	HIS237
E	HIS288
E	HIS290
E	CU402
E	CU403
E	HOH538

site_id	AF9
Number of Residues	11
Details	binding site for residue OXY E 409

Chain	Residue
E	HIS103
E	HIS157
E	HIS159
E	CU406
E	CU407
E	HOH534
F	HIS235
F	HIS237
F	HIS288
F	HIS290
F	CU403

site_id	AG1
Number of Residues	5
Details	binding site for residue CU F 401

Chain	Residue
D	HIS290
D	OXY405
F	HIS103
F	HIS105
F	HIS157

site_id	AG2
Number of Residues	4
Details	binding site for residue CU F 402

Chain	Residue
F	HIS232
F	CYS289
F	HIS294
F	MET299

site_id	AG3
Number of Residues	4
Details	binding site for residue CU F 403

Chain	Residue
E	HIS159
E	OXY409
F	HIS237
F	HIS288

site_id	AG4
Number of Residues	10
Details	binding site for residue GOL F 404

Chain	Residue
F	GLY152
F	TYR153
F	ILE179
F	VAL180
F	ARG181
F	ASP185
F	ARG245
F	THR246
F	HOH502
F	HOH504

Functional Information from PROSITE/UniProt

site_id	PS00080
Number of Residues	12
Details	MULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHvqsHsdmGM

Chain	Residue	Details
A	HIS288-MET299

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