Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3GYR

Structure of Phenoxazinone synthase from Streptomyces antibioticus reveals a new type 2 copper center.

Replaces: 2G23

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0017000	biological_process	antibiotic biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0050149	molecular_function	o-aminophenol oxidase activity
B	0005507	molecular_function	copper ion binding
B	0016491	molecular_function	oxidoreductase activity
B	0017000	biological_process	antibiotic biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0050149	molecular_function	o-aminophenol oxidase activity
C	0005507	molecular_function	copper ion binding
C	0016491	molecular_function	oxidoreductase activity
C	0017000	biological_process	antibiotic biosynthetic process
C	0046872	molecular_function	metal ion binding
C	0050149	molecular_function	o-aminophenol oxidase activity
D	0005507	molecular_function	copper ion binding
D	0016491	molecular_function	oxidoreductase activity
D	0017000	biological_process	antibiotic biosynthetic process
D	0046872	molecular_function	metal ion binding
D	0050149	molecular_function	o-aminophenol oxidase activity
E	0005507	molecular_function	copper ion binding
E	0016491	molecular_function	oxidoreductase activity
E	0017000	biological_process	antibiotic biosynthetic process
E	0046872	molecular_function	metal ion binding
E	0050149	molecular_function	o-aminophenol oxidase activity
F	0005507	molecular_function	copper ion binding
F	0016491	molecular_function	oxidoreductase activity
F	0017000	biological_process	antibiotic biosynthetic process
F	0046872	molecular_function	metal ion binding
F	0050149	molecular_function	o-aminophenol oxidase activity
G	0005507	molecular_function	copper ion binding
G	0016491	molecular_function	oxidoreductase activity
G	0017000	biological_process	antibiotic biosynthetic process
G	0046872	molecular_function	metal ion binding
G	0050149	molecular_function	o-aminophenol oxidase activity
H	0005507	molecular_function	copper ion binding
H	0016491	molecular_function	oxidoreductase activity
H	0017000	biological_process	antibiotic biosynthetic process
H	0046872	molecular_function	metal ion binding
H	0050149	molecular_function	o-aminophenol oxidase activity
I	0005507	molecular_function	copper ion binding
I	0016491	molecular_function	oxidoreductase activity
I	0017000	biological_process	antibiotic biosynthetic process
I	0046872	molecular_function	metal ion binding
I	0050149	molecular_function	o-aminophenol oxidase activity
J	0005507	molecular_function	copper ion binding
J	0016491	molecular_function	oxidoreductase activity
J	0017000	biological_process	antibiotic biosynthetic process
J	0046872	molecular_function	metal ion binding
J	0050149	molecular_function	o-aminophenol oxidase activity
K	0005507	molecular_function	copper ion binding
K	0016491	molecular_function	oxidoreductase activity
K	0017000	biological_process	antibiotic biosynthetic process
K	0046872	molecular_function	metal ion binding
K	0050149	molecular_function	o-aminophenol oxidase activity
L	0005507	molecular_function	copper ion binding
L	0016491	molecular_function	oxidoreductase activity
L	0017000	biological_process	antibiotic biosynthetic process
L	0046872	molecular_function	metal ion binding
L	0050149	molecular_function	o-aminophenol oxidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU A 1000

Chain	Residue
A	HIS524
A	CYS603
A	LEU605
A	HIS608
A	MET613

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU A 1004

Chain	Residue
A	C2O1002
A	HIS161
A	HIS527
A	HIS529
A	HOH689

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU A 1005

Chain	Residue
A	HIS434
A	HIS438
A	HIS440

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE C2O A 1002

Chain	Residue
A	HIS161
A	HIS163
A	HIS201
A	HIS203
A	HIS527
A	HIS529
A	HIS602
A	HIS604
A	CU1004

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU B 1000

Chain	Residue
B	HIS524
B	CYS603
B	LEU605
B	HIS608
B	MET613

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU B 1004

Chain	Residue
B	HIS161
B	HIS163
B	HIS527
B	HIS529
B	HOH804
B	C2O1002

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU B 1005

Chain	Residue
B	HIS434
B	HIS438
B	HIS440
B	GLN513
B	HOH4773

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE C2O B 1002

Chain	Residue
B	HIS161
B	HIS163
B	HIS201
B	HIS203
B	HIS529
B	HIS602
B	HIS604
B	CU1004

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU C 1000

Chain	Residue
C	HIS524
C	CYS603
C	HIS608
C	MET613

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU C 1004

Chain	Residue
C	HIS161
C	HIS163
C	HIS527
C	HIS529
C	HOH653
C	C2O1002

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU C 1005

Chain	Residue
C	HIS434
C	HIS438
C	HIS440

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE C2O C 1002

Chain	Residue
C	HIS161
C	HIS163
C	HIS201
C	HIS203
C	HIS527
C	HIS529
C	HIS602
C	HIS604
C	CU1004

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU D 1000

Chain	Residue
D	HIS524
D	CYS603
D	HIS608
D	MET613

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU D 1004

Chain	Residue
D	HIS161
D	HIS163
D	HIS527
D	HIS529
D	HOH665
D	C2O1002

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU D 1005

Chain	Residue
D	HIS434
D	HIS438
D	HIS440

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE C2O D 1002

Chain	Residue
D	HIS161
D	HIS163
D	HIS201
D	HIS203
D	HIS527
D	HIS529
D	HIS602
D	HIS604
D	CU1004

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU E 1000

Chain	Residue
E	HIS524
E	CYS603
E	HIS608
E	MET613

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU E 1004

Chain	Residue
E	C2O1002
E	HIS161
E	HIS163
E	HIS527
E	HIS529
E	HOH766

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU E 1005

Chain	Residue
E	HIS434
E	HIS438
E	HIS440
E	GLN513

site_id	CC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE C2O E 1002

Chain	Residue
E	HIS161
E	HIS163
E	HIS201
E	HIS203
E	HIS529
E	HIS602
E	HIS604
E	CU1004

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU F 1000

Chain	Residue
F	HIS524
F	CYS603
F	LEU605
F	HIS608
F	MET613

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU F 1004

Chain	Residue
F	HIS161
F	HIS163
F	HIS527
F	HIS529
F	C2O1002

site_id	CC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU F 1005

Chain	Residue
F	HIS434
F	HIS438
F	HIS440

site_id	CC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE C2O F 1002

Chain	Residue
F	HIS161
F	HIS163
F	HIS201
F	HIS203
F	HIS527
F	HIS529
F	HIS602
F	HIS604
F	CU1004

site_id	CC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU G 1000

Chain	Residue
G	HIS524
G	CYS603
G	LEU605
G	HIS608
G	MET613

site_id	CC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU G 1004

Chain	Residue
G	HIS161
G	HIS163
G	HIS527
G	HIS529
G	HOH661
G	C2O1002

site_id	CC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU G 1005

Chain	Residue
G	HIS434
G	HIS438
G	HIS440

site_id	DC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE C2O G 1002

Chain	Residue
G	HIS161
G	HIS163
G	HIS201
G	HIS203
G	HIS529
G	HIS602
G	HIS604
G	CU1004

site_id	DC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU H 1000

Chain	Residue
H	HIS524
H	CYS603
H	LEU605
H	HIS608
H	MET613

site_id	DC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU H 1004

Chain	Residue
H	HIS161
H	HIS163
H	HIS527
H	HIS529
H	HOH716
H	C2O1002

site_id	DC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU H 1005

Chain	Residue
H	HIS434
H	HIS438
H	HIS440
H	GLN513

site_id	DC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE C2O H 1002

Chain	Residue
H	HIS161
H	HIS163
H	HIS201
H	HIS203
H	HIS527
H	HIS529
H	HIS602
H	HIS604
H	CU1004

site_id	DC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU I 1000

Chain	Residue
I	HIS524
I	CYS603
I	LEU605
I	HIS608
I	MET613

site_id	DC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU I 1004

Chain	Residue
I	HIS161
I	HIS163
I	HIS527
I	HIS529
I	C2O1002
I	HOH1029

site_id	DC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU I 1005

Chain	Residue
I	HIS434
I	HIS438
I	HIS440

site_id	DC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE C2O I 1002

Chain	Residue
I	HIS161
I	HIS163
I	HIS201
I	HIS203
I	HIS527
I	HIS529
I	HIS602
I	HIS604
I	CU1004

site_id	EC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU J 1000

Chain	Residue
J	HIS524
J	CYS603
J	HIS608
J	MET613

site_id	EC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU J 1004

Chain	Residue
J	HIS161
J	HIS163
J	HIS527
J	HIS529
J	HOH722
J	C2O1002

site_id	EC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU J 1005

Chain	Residue
J	HIS434
J	HIS438
J	HIS440
J	GLN513

site_id	EC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE C2O J 1002

Chain	Residue
J	HIS161
J	HIS163
J	HIS201
J	HIS203
J	HIS527
J	HIS529
J	HIS602
J	HIS604
J	CU1004

site_id	EC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU K 1000

Chain	Residue
K	HIS524
K	CYS603
K	LEU605
K	HIS608
K	MET613

site_id	EC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU K 1004

Chain	Residue
K	HIS161
K	HIS163
K	HIS527
K	HIS529
K	HOH670
K	C2O1002

site_id	EC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU K 1005

Chain	Residue
K	HIS434
K	HIS438
K	HIS440

site_id	EC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE C2O K 1002

Chain	Residue
K	HIS161
K	HIS163
K	HIS201
K	HIS203
K	HIS527
K	HIS529
K	HIS602
K	HIS604
K	CU1004

site_id	EC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU L 1000

Chain	Residue
L	HIS524
L	CYS603
L	LEU605
L	HIS608
L	MET613

site_id	FC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU L 1004

Chain	Residue
L	HIS161
L	HIS163
L	HIS527
L	HIS529
L	HOH683
L	C2O1002

site_id	FC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU L 1005

Chain	Residue
L	HIS434
L	HIS438
L	HIS440

site_id	FC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE C2O L 1002

Chain	Residue
L	HIS163
L	HIS201
L	HIS203
L	HIS527
L	HIS529
L	HIS602
L	HIS604
L	CU1004

site_id	FC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 5001

Chain	Residue
A	SER359
A	GLU364
A	PHE366
A	ASN570
A	LYS575
A	GLN579
A	HOH660
A	HOH2262
A	HOH2865

site_id	FC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 5002

Chain	Residue
B	SER359
B	GLU364
B	PHE366
B	ASN570
B	GLN579
B	HOH2510
B	HOH2763
B	HOH4350

site_id	FC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 5003

Chain	Residue
C	SER359
C	GLU364
C	PHE366
C	ASN570
C	GLN579
C	HOH656
C	HOH688
C	HOH1754

site_id	FC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 5004

Chain	Residue
D	SER359
D	GLU364
D	ASN570
D	GLN579
D	HOH696
D	HOH1120
D	HOH1675

site_id	FC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL E 5005

Chain	Residue
E	SER359
E	GLU364
E	PHE366
E	ASN570
E	LYS575
E	GLN579
E	HOH740
E	HOH3585

site_id	FC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL F 5006

Chain	Residue
F	SER359
F	GLU364
F	PHE366
F	ASN570
F	GLN579
F	HOH1066
F	HOH1444

site_id	GC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL G 5007

Chain	Residue
G	SER359
G	GLU364
G	PHE366
G	ASN570
G	LYS575
G	GLN579
G	HOH658
G	HOH1116

site_id	GC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL H 5008

Chain	Residue
H	SER359
H	GLU364
H	PHE366
H	ASN570
H	GLN579
H	HOH658
H	HOH1264

site_id	GC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL I 5009

Chain	Residue
I	SER359
I	GLU364
I	PHE366
I	ASN570
I	GLN579
I	HOH924
I	HOH2896

site_id	GC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL J 5010

Chain	Residue
J	SER359
J	GLU364
J	PHE366
J	ASN570
J	GLN579
J	HOH688
J	HOH1061
J	HOH1789

site_id	GC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL K 5011

Chain	Residue
K	SER359
K	GLU364
K	PHE366
K	ASN570
K	LYS575
K	GLN579
K	HOH751
K	HOH929

site_id	GC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL L 5012

Chain	Residue
L	SER359
L	GLU364
L	PHE366
L	ASN570
L	LYS575
L	GLN579
L	HOH661
L	HOH1023

Functional Information from PROSITE/UniProt

site_id	PS00079
Number of Residues	21
Details	MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GrFmYhChLLehEdMGMmrpF

Chain	Residue	Details
A	GLY597-PHE617

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

Chain	Residue	Details
A	HIS602-MET613

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1644
Details	Domain: {"description":"Plastocyanin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1524
Details	Domain: {"description":"Plastocyanin-like 2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	240
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	60
Details	Binding site: {"description":"type 2 copper site","evidences":[{"source":"PubMed","id":"16584173","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	72
Details	Binding site: {"description":"type 3 copper site","evidences":[{"source":"PubMed","id":"16584173","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	48
Details	Binding site: {"description":"type 1 copper site","evidences":[{"source":"PubMed","id":"16584173","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1a65

Chain	Residue	Details
A	CYS603
A	HIS602
A	HIS604

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1a65

Chain	Residue	Details
J	CYS603
J	HIS602
J	HIS604

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1a65

Chain	Residue	Details
K	CYS603
K	HIS602
K	HIS604

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1a65

Chain	Residue	Details
L	CYS603
L	HIS602
L	HIS604

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1a65

Chain	Residue	Details
B	CYS603
B	HIS602
B	HIS604

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1a65

Chain	Residue	Details
C	CYS603
C	HIS602
C	HIS604

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1a65

Chain	Residue	Details
D	CYS603
D	HIS602
D	HIS604

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1a65

Chain	Residue	Details
E	CYS603
E	HIS602
E	HIS604

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1a65

Chain	Residue	Details
F	CYS603
F	HIS602
F	HIS604

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1a65

Chain	Residue	Details
G	CYS603
G	HIS602
G	HIS604

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1a65

Chain	Residue	Details
H	CYS603
H	HIS602
H	HIS604

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1a65

Chain	Residue	Details
I	CYS603
I	HIS602
I	HIS604

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