Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3FZN

Intermediate analogue in benzoylformate decarboxylase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0009056	biological_process	catabolic process
A	0016831	molecular_function	carboxy-lyase activity
A	0018924	biological_process	mandelate metabolic process
A	0019596	biological_process	mandelate catabolic process
A	0019752	biological_process	carboxylic acid metabolic process
A	0030976	molecular_function	thiamine pyrophosphate binding
A	0046872	molecular_function	metal ion binding
A	0050695	molecular_function	benzoylformate decarboxylase activity
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0009056	biological_process	catabolic process
B	0016831	molecular_function	carboxy-lyase activity
B	0018924	biological_process	mandelate metabolic process
B	0019596	biological_process	mandelate catabolic process
B	0019752	biological_process	carboxylic acid metabolic process
B	0030976	molecular_function	thiamine pyrophosphate binding
B	0046872	molecular_function	metal ion binding
B	0050695	molecular_function	benzoylformate decarboxylase activity
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0009056	biological_process	catabolic process
C	0016831	molecular_function	carboxy-lyase activity
C	0018924	biological_process	mandelate metabolic process
C	0019596	biological_process	mandelate catabolic process
C	0019752	biological_process	carboxylic acid metabolic process
C	0030976	molecular_function	thiamine pyrophosphate binding
C	0046872	molecular_function	metal ion binding
C	0050695	molecular_function	benzoylformate decarboxylase activity
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0009056	biological_process	catabolic process
D	0016831	molecular_function	carboxy-lyase activity
D	0018924	biological_process	mandelate metabolic process
D	0019596	biological_process	mandelate catabolic process
D	0019752	biological_process	carboxylic acid metabolic process
D	0030976	molecular_function	thiamine pyrophosphate binding
D	0046872	molecular_function	metal ion binding
D	0050695	molecular_function	benzoylformate decarboxylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	BINDING SITE FOR RESIDUE D7K A 601

Chain	Residue
A	HIS281
A	TYR433
A	ASN455
A	THR457
A	TYR458
A	GLY459
A	ALA460
A	LEU461
A	PHE464
A	HOH545
A	MG605
A	THR377
A	HOH1986
B	ASN23
B	PRO24
B	GLY25
B	SER26
B	GLU47
B	HIS70
B	ASN77
B	LEU110
A	SER378
A	GLY401
A	LEU403
A	GLY427
A	ASP428
A	GLY429
A	SER430

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 605

Chain	Residue
A	ASP428
A	ASN455
A	THR457
A	HOH545
A	D7K601

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 704

Chain	Residue
A	ASP187
D	ARG184

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 705

Chain	Residue
A	ARG184
D	ASP187

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL A 709

Chain	Residue
A	ASN117
A	LEU118
A	ARG120
B	ASN117
B	LEU118
B	ARG120

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CL A 710

Chain	Residue
A	GLN421
A	ALA510
A	LEU511
A	ALA513
A	HOH1992
A	HOH2008
A	HOH2763

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 712

Chain	Residue
A	GLN287
A	LEU289
A	LYS290
A	PRO291
A	HOH2022
A	HOH2612
D	GLN170
D	HIS172
D	HIS173

site_id	AC8
Number of Residues	28
Details	BINDING SITE FOR RESIDUE D7K B 602

Chain	Residue
A	ASN23
A	PRO24
A	GLY25
A	SER26
A	GLU47
A	HIS70
A	ASN77
A	LEU110
B	HIS281
B	THR377
B	SER378
B	GLY401
B	LEU403
B	GLY427
B	ASP428
B	GLY429
B	SER430
B	TYR433
B	ASN455
B	THR457
B	TYR458
B	GLY459
B	ALA460
B	LEU461
B	PHE464
B	MG606
B	HOH655
B	HOH849

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 606

Chain	Residue
B	ASP428
B	ASN455
B	THR457
B	D7K602
B	HOH655

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL B 701

Chain	Residue
B	ASP187
C	ARG184

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL B 702

Chain	Residue
B	ARG184
C	ASP187

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CL B 703

Chain	Residue
B	ALA513
B	HOH1774
B	HOH1990
B	HOH2159
B	HOH2859
B	GLN421
B	ALA510
B	LEU511

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL B 708

Chain	Residue
B	ASP114
B	ALA115
B	ALA116
B	HOH1504
B	HOH2838

site_id	BC5
Number of Residues	28
Details	BINDING SITE FOR RESIDUE D7K C 604

Chain	Residue
C	HIS281
C	THR377
C	SER378
C	GLY401
C	LEU403
C	GLY427
C	ASP428
C	GLY429
C	SER430
C	TYR433
C	ASN455
C	THR457
C	TYR458
C	GLY459
C	ALA460
C	LEU461
C	PHE464
C	HOH539
C	MG607
C	HOH1979
D	ASN23
D	PRO24
D	GLY25
D	SER26
D	GLU47
D	HIS70
D	ASN77
D	LEU110

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 607

Chain	Residue
C	ASP428
C	ASN455
C	THR457
C	HOH539
C	D7K604

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL C 707

Chain	Residue
C	GLN421
C	ALA510
C	LEU511
C	ALA513
C	HOH839
C	HOH2021

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL C 711

Chain	Residue
C	ASN117
C	LEU118
C	ARG120
D	ASN117
D	LEU118
D	ARG120

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 C 713

Chain	Residue
B	GLN170
B	HIS172
B	HIS173
C	GLN287
C	LEU289
C	LYS290
C	PRO291

site_id	CC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 C 714

Chain	Residue
B	ASP166
B	GLN287
B	LEU289
B	LYS290
B	PRO291
C	GLN170
C	HIS172
C	HIS173
C	HOH2139
C	HOH2879
C	HOH2880

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG C 715

Chain	Residue
C	ASP18
C	ASP38
C	PHE39
C	HOH2929

site_id	CC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PEG C 716

Chain	Residue
A	GLN335
C	ALA218
C	VAL221
C	PRO243
C	PRO392
C	HOH710
C	HOH859
C	HOH1615
C	HOH2069
C	HOH2959
C	HOH3178

site_id	CC4
Number of Residues	28
Details	BINDING SITE FOR RESIDUE D7K D 603

Chain	Residue
C	ASN23
C	PRO24
C	GLY25
C	SER26
C	GLU47
C	HIS70
C	ASN77
C	LEU110
D	HIS281
D	THR377
D	SER378
D	GLY401
D	LEU403
D	GLY427
D	ASP428
D	GLY429
D	SER430
D	TYR433
D	ASN455
D	THR457
D	TYR458
D	GLY459
D	ALA460
D	LEU461
D	PHE464
D	HOH607
D	MG608
D	HOH689

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 608

Chain	Residue
D	ASP428
D	ASN455
D	THR457
D	D7K603
D	HOH607

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL D 706

Chain	Residue
D	GLN421
D	ALA510
D	LEU511
D	ALA513
D	HOH733
D	HOH2002

site_id	CC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG D 718

Chain	Residue
D	ASP18
D	GLU37
D	ASP38
D	PHE39
D	HOH2935
D	HOH3202

Functional Information from PROSITE/UniProt

site_id	PS00187
Number of Residues	20
Details	TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGvqlaePerqvIaViGDGS

Chain	Residue	Details
A	ILE411-SER430

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING:

Chain	Residue	Details
A	ASN117
B	ASP428
B	ASN455
B	THR457
C	ASN117
C	LEU118
C	ARG120
C	ASP428
C	ASN455
C	THR457
D	ASN117
A	LEU118
D	LEU118
D	ARG120
D	ASP428
D	ASN455
D	THR457
A	ARG120
A	ASP428
A	ASN455
A	THR457
B	ASN117
B	LEU118
B	ARG120

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU28
A	HIS281
A	HIS70

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

Chain	Residue	Details
B	GLU28
B	HIS281
B	HIS70

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

Chain	Residue	Details
C	GLU28
C	HIS281
C	HIS70

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

Chain	Residue	Details
D	GLU28
D	HIS281
D	HIS70

site_id	MCSA1
Number of Residues	7
Details	M-CSA 220

Chain	Residue	Details
A	GLY25	electrostatic stabiliser, hydrogen bond donor
A	SER26	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
A	GLU28	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLU47	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS70	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	HIS281	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLY401	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA2
Number of Residues	7
Details	M-CSA 220

Chain	Residue	Details
B	GLY25	electrostatic stabiliser, hydrogen bond donor
B	SER26	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
B	GLU28	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLU47	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS70	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	HIS281	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLY401	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA3
Number of Residues	7
Details	M-CSA 220

Chain	Residue	Details
C	GLY25	electrostatic stabiliser, hydrogen bond donor
C	SER26	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
C	GLU28	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	GLU47	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	HIS70	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	HIS281	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	GLY401	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA4
Number of Residues	7
Details	M-CSA 220

Chain	Residue	Details
D	GLY25	electrostatic stabiliser, hydrogen bond donor
D	SER26	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
D	GLU28	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	GLU47	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	HIS70	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	HIS281	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	GLY401	electrostatic stabiliser, hydrogen bond acceptor

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