Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1PN0

Phenol hydroxylase from Trichosporon cutaneum

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016709	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
A	0018662	molecular_function	phenol 2-monooxygenase activity
A	0019336	biological_process	phenol-containing compound catabolic process
A	0071949	molecular_function	FAD binding
B	0004497	molecular_function	monooxygenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0016709	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
B	0018662	molecular_function	phenol 2-monooxygenase activity
B	0019336	biological_process	phenol-containing compound catabolic process
B	0071949	molecular_function	FAD binding
C	0004497	molecular_function	monooxygenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016709	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
C	0018662	molecular_function	phenol 2-monooxygenase activity
C	0019336	biological_process	phenol-containing compound catabolic process
C	0071949	molecular_function	FAD binding
D	0004497	molecular_function	monooxygenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016709	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
D	0018662	molecular_function	phenol 2-monooxygenase activity
D	0019336	biological_process	phenol-containing compound catabolic process
D	0071949	molecular_function	FAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CL A 6001

Chain	Residue
A	LYS65
A	GLY68
A	LEU69
A	ALA70
A	ASP71
A	HOH6561
A	HOH6576

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL B 6002

Chain	Residue
B	LEU69
B	ALA70
B	ASP71
B	HOH1245
B	LYS65
B	GLY68

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CL C 6003

Chain	Residue
C	LYS65
C	GLY68
C	LEU69
C	ALA70
C	ASP71
C	HOH6600
C	HOH6615

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CL D 6004

Chain	Residue
D	LYS65
D	GLY68
D	LEU69
D	ALA70
D	ASP71
D	HOH6602
D	HOH6617

site_id	AC5
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD A 6011

Chain	Residue
A	VAL13
A	GLY14
A	GLY16
A	PRO17
A	ALA18
A	ASP42
A	LYS43
A	ARG44
A	ALA53
A	GLN117
A	LEU142
A	PRO144
A	CYS224
A	ASP225
A	GLY226
A	ARG287
A	TYR289
A	TRP332
A	GLY356
A	ASP357
A	PRO364
A	GLY369
A	MET370
A	SER373
A	HOH6022
A	HOH6030
A	HOH6051
A	HOH6067
A	HOH6093
A	HOH6103
A	HOH6120
A	HOH6403
A	HOH6408
A	HOH6415
A	HOH6542
A	HOH6585
A	HOH6586

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE IPH A 6012

Chain	Residue
A	ASP54
A	GLN112
A	VAL114
A	MET277
A	ILE279
A	TYR289
A	PRO364
A	LYS365
A	ALA366
A	GLY367

site_id	AC7
Number of Residues	35
Details	BINDING SITE FOR RESIDUE FAD B 6021

Chain	Residue
B	HOH706
B	HOH722
B	HOH748
B	HOH758
B	HOH1057
B	HOH1062
B	HOH1069
B	HOH1215
B	HOH1254
B	HOH1255
B	GLY14
B	GLY16
B	PRO17
B	ALA18
B	ASP42
B	LYS43
B	ARG44
B	ALA53
B	GLN117
B	LEU142
B	PRO144
B	CYS224
B	ASP225
B	GLY226
B	ARG287
B	TYR289
B	TRP332
B	GLY356
B	ASP357
B	PRO364
B	GLY369
B	MET370
B	SER373
B	HOH677
B	HOH685

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE IPH B 6022

Chain	Residue
B	ASP54
B	GLN112
B	VAL114
B	MET277
B	ILE279
B	TYR289
B	PRO364
B	ALA366
B	GLY367

site_id	AC9
Number of Residues	38
Details	BINDING SITE FOR RESIDUE FAD C 6031

Chain	Residue
C	GLY14
C	GLY16
C	PRO17
C	ALA18
C	ASP42
C	LYS43
C	ARG44
C	ASN50
C	GLN52
C	ALA53
C	ASP54
C	GLY55
C	LEU142
C	PRO144
C	ARG189
C	CYS224
C	ASP225
C	GLY226
C	ARG287
C	TYR289
C	GLY356
C	ASP357
C	PRO364
C	GLY367
C	GLN368
C	GLY369
C	MET370
C	ASN371
C	SER373
C	IPH6032
C	HOH6044
C	HOH6052
C	HOH6073
C	HOH6099
C	HOH6102
C	HOH6149
C	HOH6438
C	HOH6443

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE IPH C 6032

Chain	Residue
C	ASP54
C	GLN112
C	VAL114
C	MET277
C	TYR289
C	PRO364
C	ALA366
C	GLY367
C	FAD6031

site_id	BC2
Number of Residues	39
Details	BINDING SITE FOR RESIDUE FAD D 6041

Chain	Residue
D	GLY14
D	GLY16
D	PRO17
D	ALA18
D	ASP42
D	LYS43
D	ARG44
D	ASN50
D	GLN52
D	ALA53
D	ASP54
D	GLY55
D	LEU142
D	ILE143
D	PRO144
D	ARG189
D	CYS224
D	ASP225
D	GLY226
D	ARG287
D	TYR289
D	GLY356
D	ASP357
D	PRO364
D	GLY367
D	GLN368
D	GLY369
D	MET370
D	ASN371
D	SER373
D	IPH6042
D	HOH6062
D	HOH6070
D	HOH6091
D	HOH6117
D	HOH6120
D	HOH6160
D	HOH6462
D	HOH6467

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE IPH D 6042

Chain	Residue
D	ASP54
D	GLN112
D	MET277
D	ILE279
D	TYR289
D	PRO364
D	ALA366
D	GLY367
D	FAD6041

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	60
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12925790","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9634698","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FOH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PN0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PDB","id":"1FOH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PN0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP54
A	ARG281
A	TYR289

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

Chain	Residue	Details
B	ASP54
B	ARG281
B	TYR289

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

Chain	Residue	Details
C	ASP54
C	ARG281
C	TYR289

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

Chain	Residue	Details
D	ASP54
D	ARG281
D	TYR289

site_id	MCSA1
Number of Residues	4
Details	M-CSA 551

Chain	Residue	Details
A	ASP54	electrostatic stabiliser
A	ARG281	electrostatic stabiliser
A	TYR289	steric role
A	PRO364	activator, electrostatic stabiliser

site_id	MCSA2
Number of Residues	4
Details	M-CSA 551

Chain	Residue	Details
B	ASP54	electrostatic stabiliser
B	ARG281	electrostatic stabiliser
B	TYR289	steric role
B	PRO364	activator, electrostatic stabiliser

site_id	MCSA3
Number of Residues	4
Details	M-CSA 551

Chain	Residue	Details
C	ASP54	electrostatic stabiliser
C	ARG281	electrostatic stabiliser
C	TYR289	steric role
C	PRO364	activator, electrostatic stabiliser

site_id	MCSA4
Number of Residues	4
Details	M-CSA 551

Chain	Residue	Details
D	ASP54	electrostatic stabiliser
D	ARG281	electrostatic stabiliser
D	TYR289	steric role
D	PRO364	activator, electrostatic stabiliser

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