Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1FOH

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	29
Details	BINDING SITE FOR RESIDUE FAD A 801

Chain	Residue
A	VAL13
A	GLN117
A	PRO144
A	CYS224
A	ASP225
A	GLY226
A	ARG287
A	TYR289
A	TRP332
A	GLY356
A	ASP357
A	GLY14
A	PRO364
A	GLY369
A	MET370
A	SER373
A	HOH806
A	HOH894
A	HOH896
A	HOH951
A	HOH970
A	HOH998
A	GLY16
A	PRO17
A	ALA18
A	ASP42
A	LYS43
A	ARG44
A	ALA53

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE IPH A 802

Chain	Residue
A	ASP54
A	GLN112
A	ARG265
A	ILE279
A	TYR289
A	PRO364
A	ALA366
A	GLY367
A	HOH1092

site_id	AC3
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD B 801

Chain	Residue
B	GLY14
B	GLY16
B	PRO17
B	ALA18
B	ASP42
B	LYS43
B	ARG44
B	ALA53
B	GLN117
B	PRO144
B	CYS224
B	ASP225
B	GLY226
B	VAL250
B	ARG287
B	TYR289
B	GLY356
B	ASP357
B	PRO364
B	GLY369
B	MET370
B	SER373
B	HOH806
B	HOH897
B	HOH918
B	HOH937
B	HOH947
B	HOH1005
B	HOH1037

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE IPH B 802

Chain	Residue
B	ASP54
B	GLN112
B	ARG265
B	ILE279
B	TYR289
B	PRO364
B	ALA366
B	GLY367

site_id	AC5
Number of Residues	35
Details	BINDING SITE FOR RESIDUE FAD C 801

Chain	Residue
C	MET370
C	ASN371
C	SER373
C	IPH802
C	HOH808
C	HOH869
C	HOH916
C	HOH1051
C	HOH1069
C	HOH1072
C	HOH1093
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	CYS224
C	ASP225
C	GLY226
C	TYR289
C	GLY356
C	ASP357
C	PRO364
C	GLY367
C	GLN368
C	GLY369

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE IPH C 802

Chain	Residue
C	ASP54
C	GLN112
C	VAL114
C	ARG265
C	TYR289
C	PRO364
C	ALA366
C	GLY367
C	FAD801

site_id	AC7
Number of Residues	35
Details	BINDING SITE FOR RESIDUE FAD D 801

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	PRO144
D	ASN191
D	CYS224
D	ASP225
D	GLY226
D	TYR289
D	GLY356
D	ASP357
D	GLY367
D	GLN368
D	GLY369
D	MET370
D	ASN371
D	SER373
D	IPH802
D	HOH807
D	HOH868
D	HOH921
D	HOH933
D	HOH935
D	HOH1010
D	HOH1051

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE IPH D 802

Chain	Residue
D	ASP54
D	GLN112
D	VAL114
D	TYR289
D	PRO364
D	ALA366
D	GLY367
D	FAD801

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	4
Details	a catalytic site defined by CSA, PubMed 12427024, 11591156, 9634698

Chain	Residue	Details
A	PRO364
A	ASP54
A	ARG281
A	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)