Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3T63

Axial Ligand Swapping In Double Mutant Maintains Intradiol-cleavage Chemistry in Protocatechuate 3,4-Dioxygenase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005506	molecular_function	iron ion binding
A	0008199	molecular_function	ferric iron binding
A	0009056	biological_process	catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
A	0042952	biological_process	beta-ketoadipate pathway
A	0051213	molecular_function	dioxygenase activity
B	0003824	molecular_function	catalytic activity
B	0005506	molecular_function	iron ion binding
B	0008199	molecular_function	ferric iron binding
B	0009056	biological_process	catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
B	0042952	biological_process	beta-ketoadipate pathway
B	0051213	molecular_function	dioxygenase activity
C	0003824	molecular_function	catalytic activity
C	0005506	molecular_function	iron ion binding
C	0008199	molecular_function	ferric iron binding
C	0009056	biological_process	catabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
C	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
C	0042952	biological_process	beta-ketoadipate pathway
C	0051213	molecular_function	dioxygenase activity
M	0003824	molecular_function	catalytic activity
M	0005506	molecular_function	iron ion binding
M	0008199	molecular_function	ferric iron binding
M	0016491	molecular_function	oxidoreductase activity
M	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
M	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
M	0019619	biological_process	3,4-dihydroxybenzoate catabolic process
M	0042952	biological_process	beta-ketoadipate pathway
M	0046872	molecular_function	metal ion binding
M	0051213	molecular_function	dioxygenase activity
N	0003824	molecular_function	catalytic activity
N	0005506	molecular_function	iron ion binding
N	0008199	molecular_function	ferric iron binding
N	0016491	molecular_function	oxidoreductase activity
N	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
N	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
N	0019619	biological_process	3,4-dihydroxybenzoate catabolic process
N	0042952	biological_process	beta-ketoadipate pathway
N	0046872	molecular_function	metal ion binding
N	0051213	molecular_function	dioxygenase activity
O	0003824	molecular_function	catalytic activity
O	0005506	molecular_function	iron ion binding
O	0008199	molecular_function	ferric iron binding
O	0016491	molecular_function	oxidoreductase activity
O	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
O	0018578	molecular_function	protocatechuate 3,4-dioxygenase activity
O	0019619	biological_process	3,4-dihydroxybenzoate catabolic process
O	0042952	biological_process	beta-ketoadipate pathway
O	0046872	molecular_function	metal ion binding
O	0051213	molecular_function	dioxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BME A 201

Chain	Residue
A	TYR56
A	ASP57
A	GLY60
A	ARG188
A	ILE189
A	GLN190
A	GLY191
A	GLU192

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 202

Chain	Residue
A	THR169
A	LEU170
A	ILE171
A	ARG184
A	PHE185
A	ASP186
A	ARG188
A	HOH955
A	GLU168

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 203

Chain	Residue
A	ASN37
A	THR105
A	HIS107
A	HOH682

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 201

Chain	Residue
B	GLU168
B	THR169
B	ILE171
B	ARG184
B	PHE185
B	ASP186
B	ARG188

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 202

Chain	Residue
B	ASN37
B	ARG38
B	THR105
B	HIS107

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 201

Chain	Residue
C	THR169
C	ILE171
C	ARG184
C	PHE185
C	ASP186
C	ARG188
C	HOH954
C	HOH1492

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 202

Chain	Residue
C	ASN37
C	THR105
C	HIS107

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BME M 1

Chain	Residue
M	TYR408
M	ARG457
M	HIS460
M	TYR462
M	BME542
M	FE600
M	HOH613
M	HOH1559

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME M 539

Chain	Residue
M	PHE356
M	CYS429
M	LEU430
M	HOH568

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BME M 540

Chain	Residue
M	ARG450
M	PRO453
M	HOH1460
M	HOH1545
N	HOH145
N	SER338
N	ILE339
N	PRO340

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL M 541

Chain	Residue
M	GLN503
M	ILE505
M	ARG522
M	PHE523
M	ASP524

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 M 7

Chain	Residue
M	ARG383

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BME M 542

Chain	Residue
A	PRO15
A	ARG133
A	HOH1482
M	BME1
M	HOH296
M	TYR324
M	THR326
M	TRP449
M	HOH1488

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BME M 543

Chain	Residue
A	PHE200
M	ILE310
M	ILE339
M	PRO340
M	GLN341
M	HOH547
O	PRO453
O	PRO515

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE M 600

Chain	Residue
M	BME1
M	TYR408
M	HIS460
M	TYR462
M	HOH1559

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BME N 1

Chain	Residue
B	TYR16
N	TYR408
N	ARG457
N	TYR462
N	BME540
N	HOH577
N	FE600
N	HOH1560

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME N 539

Chain	Residue
N	PHE356
N	CYS429
N	LEU430
N	HOH700
N	HOH1102

site_id	BC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BME N 540

Chain	Residue
B	PRO15
B	ARG133
N	BME1
N	HOH65
N	TYR324
N	THR326
N	TRP449
N	HOH1484
N	HOH1536

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE N 600

Chain	Residue
N	BME1
N	TYR408
N	HIS460
N	TYR462
N	HOH1560

site_id	CC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE BME O 1

Chain	Residue
C	TYR16
O	TYR408
O	TRP449
O	ARG457
O	HIS460
O	TYR462
O	BME539
O	BME540
O	FE600
O	HOH654
O	HOH1561
O	HOH1566

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BME O 539

Chain	Residue
C	PRO15
O	BME1
O	TRP449
O	ARG450
O	BME540
O	HOH1566

site_id	CC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BME O 540

Chain	Residue
C	PRO15
C	ARG133
O	BME1
O	HOH143
O	TYR324
O	THR326
O	TRP449
O	BME539

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE O 600

Chain	Residue
O	BME1
O	TYR408
O	HIS460
O	TYR462
O	HOH1561

Functional Information from PROSITE/UniProt

site_id	PS00083
Number of Residues	29
Details	INTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. LlGqVydgnGhlVrdsfLEVwqadanGeY

Chain	Residue	Details
A	LEU51-TYR79
M	VAL380-TYR408

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7990141","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 936

Chain

Residue

Details

site_id	MCSA2
Number of Residues	5
Details	M-CSA 936

Chain

Residue

Details

site_id	MCSA3
Number of Residues	5
Details	M-CSA 936

Chain

Residue

Details

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