Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6JU1

p-Hydroxybenzoate hydroxylase Y385F mutant complexed with 3,4-dihydroxybenzoate

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	0018659	molecular_function	4-hydroxybenzoate 3-monooxygenase activity
A	0043639	biological_process	benzoate catabolic process
A	0043640	biological_process	benzoate catabolic process via hydroxylation
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0071949	molecular_function	FAD binding
A	0106356	molecular_function	4-hydroxybenzoate 3-monooxygenase (NADPH) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	37
Details	binding site for residue FAD A 401

Chain	Residue
A	GLY9
A	ARG44
A	ALA45
A	GLY46
A	VAL47
A	GLN102
A	VAL127
A	CYS158
A	ASP159
A	GLY160
A	GLY163
A	GLY11
A	GLY285
A	ASP286
A	ALA296
A	LYS297
A	GLY298
A	LEU299
A	ASN300
A	DHB402
A	BR409
A	HOH571
A	PRO12
A	HOH615
A	HOH616
A	HOH625
A	HOH628
A	HOH651
A	HOH667
A	HOH676
A	HOH688
A	SER13
A	GLU32
A	ARG33
A	GLN34
A	VAL39
A	ARG42

site_id	AC2
Number of Residues	13
Details	binding site for residue DHB A 402

Chain	Residue
A	GLY46
A	VAL47
A	LEU199
A	TYR201
A	LEU210
A	SER212
A	ARG214
A	ARG220
A	TYR222
A	PRO293
A	THR294
A	ALA296
A	FAD401

site_id	AC3
Number of Residues	7
Details	binding site for residue GOL A 405

Chain	Residue
A	ARG341
A	TRP345
A	TYR371
A	THR380
A	ILE381
A	ASN384
A	HOH505

site_id	AC4
Number of Residues	9
Details	binding site for residue GOL A 406

Chain	Residue
A	GLU49
A	GLN50
A	GLY51
A	LYS95
A	ARG335
A	VAL386
A	GLY387
A	TYR390
A	HOH542

site_id	AC5
Number of Residues	4
Details	binding site for residue PG4 A 407

Chain	Residue
A	HOH502
A	HOH502
A	HOH536
A	HOH536

site_id	AC6
Number of Residues	14
Details	binding site for residue P33 A 408

Chain	Residue
A	TRP344
A	TRP344
A	TRP345
A	SER348
A	SER348
A	VAL349
A	PHE353
A	PHE353
A	GLN364
A	GLU367
A	HOH601
A	HOH601
A	HOH801
A	HOH801

site_id	AC7
Number of Residues	4
Details	binding site for residue BR A 409

Chain	Residue
A	PRO293
A	LYS297
A	GLY298
A	FAD401

site_id	AC8
Number of Residues	5
Details	binding site for residue BR A 410

Chain	Residue
A	ILE43
A	ALA45
A	GLN102
A	THR103
A	ARG214

site_id	AC9
Number of Residues	16
Details	binding site for residues GOL A 403 and GOL A 404

Chain	Residue
A	ALA171
A	ALA171
A	GLU178
A	GLU178
A	PHE271
A	PHE271
A	HOH530
A	HOH530
A	HOH557
A	HOH635
A	ARG166
A	ARG166
A	GLN167
A	GLN167
A	PRO170
A	PRO170

site_id	AD1
Number of Residues	16
Details	binding site for residues GOL A 403 and GOL A 404

Chain	Residue
A	ARG166
A	ARG166
A	GLN167
A	GLN167
A	PRO170
A	PRO170
A	ALA171
A	ALA171
A	GLU178
A	GLU178
A	PHE271
A	PHE271
A	HOH530
A	HOH530
A	HOH557
A	HOH635

site_id	AD2
Number of Residues	16
Details	binding site for residues GOL A 403 and GOL A 404

Chain	Residue
A	ARG166
A	ARG166
A	GLN167
A	GLN167
A	PRO170
A	PRO170
A	ALA171
A	ALA171
A	GLU178
A	GLU178
A	PHE271
A	PHE271
A	HOH530
A	HOH530
A	HOH557
A	HOH635

site_id	AD3
Number of Residues	16
Details	binding site for residues GOL A 403 and GOL A 404

Chain	Residue
A	ARG166
A	ARG166
A	GLN167
A	GLN167
A	PRO170
A	PRO170
A	ALA171
A	ALA171
A	GLU178
A	GLU178
A	PHE271
A	PHE271
A	HOH530
A	HOH530
A	HOH557
A	HOH635

site_id	AD4
Number of Residues	16
Details	binding site for residues GOL A 403 and GOL A 404

Chain	Residue
A	ARG166
A	ARG166
A	GLN167
A	GLN167
A	PRO170
A	PRO170
A	ALA171
A	ALA171
A	GLU178
A	GLU178
A	PHE271
A	PHE271
A	HOH530
A	HOH530
A	HOH557
A	HOH635

site_id	AD5
Number of Residues	16
Details	binding site for residues GOL A 403 and GOL A 404

Chain	Residue
A	ARG166
A	ARG166
A	GLN167
A	GLN167
A	PRO170
A	PRO170
A	ALA171
A	ALA171
A	GLU178
A	GLU178
A	PHE271
A	PHE271
A	HOH530
A	HOH530
A	HOH557
A	HOH635

site_id	AD6
Number of Residues	16
Details	binding site for residues GOL A 403 and GOL A 404

Chain	Residue
A	ARG166
A	ARG166
A	GLN167
A	GLN167
A	PRO170
A	PRO170
A	ALA171
A	ALA171
A	GLU178
A	GLU178
A	PHE271
A	PHE271
A	HOH530
A	HOH530
A	HOH557
A	HOH635

site_id	AD7
Number of Residues	16
Details	binding site for residues GOL A 403 and GOL A 404

Chain	Residue
A	ARG166
A	ARG166
A	GLN167
A	GLN167
A	PRO170
A	PRO170
A	ALA171
A	ALA171
A	GLU178
A	GLU178
A	PHE271
A	PHE271
A	HOH530
A	HOH530
A	HOH557
A	HOH635

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10600126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11805318","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15924424","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7939628","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8312276","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8555229","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10600126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15924424","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7939628","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8312276","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8555229","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"8312276","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 131

Chain	Residue	Details
A	HIS72	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	TYR201	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	PRO293	electrostatic stabiliser, hydrogen bond acceptor
A	LYS297	attractive charge-charge interaction, electrostatic stabiliser, steric role
A	PHE385	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

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