Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5DEI

BENZOYLFORMATE DECARBOXYLASE FROM PSEUDOMONAS PUTIDA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0003984	molecular_function	acetolactate synthase activity
A	0016829	molecular_function	lyase activity
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	0050660	molecular_function	flavin adenine dinucleotide binding
A	0050695	molecular_function	benzoylformate decarboxylase activity
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0003984	molecular_function	acetolactate synthase activity
B	0016829	molecular_function	lyase activity
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	0050660	molecular_function	flavin adenine dinucleotide binding
B	0050695	molecular_function	benzoylformate decarboxylase activity
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0003984	molecular_function	acetolactate synthase activity
C	0016829	molecular_function	lyase activity
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	0050660	molecular_function	flavin adenine dinucleotide binding
C	0050695	molecular_function	benzoylformate decarboxylase activity
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0003984	molecular_function	acetolactate synthase activity
D	0016829	molecular_function	lyase activity
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	0050660	molecular_function	flavin adenine dinucleotide binding
D	0050695	molecular_function	benzoylformate decarboxylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue BCT A 601

Chain	Residue
A	SER27
A	HIS71
A	LEU111
A	HOH1106
C	HIS282
C	TPP602

site_id	AC2
Number of Residues	23
Details	binding site for residue TPP A 602

Chain	Residue
A	LEU404
A	GLY428
A	ASP429
A	GLY430
A	SER431
A	TYR434
A	ASN456
A	THR458
A	TYR459
A	GLY460
A	ALA461
A	CA607
A	HOH757
C	ASN24
C	PRO25
C	GLY26
C	GLU48
C	HIS71
C	ASN78
C	BCT601
A	THR378
A	SER379
A	GLY402

site_id	AC3
Number of Residues	6
Details	binding site for residue MG A 603

Chain	Residue
A	ASN118
A	LEU119
A	ARG121
C	ASN118
C	LEU119
C	ARG121

site_id	AC4
Number of Residues	3
Details	binding site for residue MG A 604

Chain	Residue
A	LYS497
A	HOH1241
D	GLN494

site_id	AC5
Number of Residues	3
Details	binding site for residue MG A 605

Chain	Residue
A	ARG185
A	HOH871
D	ASP188

site_id	AC6
Number of Residues	2
Details	binding site for residue CA A 606

Chain	Residue
A	ASP188
D	ARG185

site_id	AC7
Number of Residues	5
Details	binding site for residue CA A 607

Chain	Residue
A	ASP429
A	ASN456
A	THR458
A	TPP602
A	HOH752

site_id	AC8
Number of Residues	7
Details	binding site for residue BCT B 601

Chain	Residue
B	SER27
B	HIS71
B	LEU111
B	HOH1107
D	HIS282
D	PHE465
D	TPP602

site_id	AC9
Number of Residues	23
Details	binding site for residue TPP B 602

Chain	Residue
B	THR378
B	SER379
B	GLY402
B	LEU404
B	GLY428
B	ASP429
B	GLY430
B	SER431
B	TYR434
B	ASN456
B	THR458
B	TYR459
B	GLY460
B	ALA461
B	CA607
B	HOH711
B	HOH765
D	ASN24
D	PRO25
D	GLU48
D	HIS71
D	ASN78
D	BCT601

site_id	AD1
Number of Residues	6
Details	binding site for residue MG B 603

Chain	Residue
B	ASN118
B	LEU119
B	ARG121
D	ASN118
D	LEU119
D	ARG121

site_id	AD2
Number of Residues	3
Details	binding site for residue MG B 604

Chain	Residue
B	ARG185
B	HOH956
C	ASP188

site_id	AD3
Number of Residues	4
Details	binding site for residue MG B 605

Chain	Residue
B	LYS497
B	HOH970
B	HOH1042
C	GLN494

site_id	AD4
Number of Residues	4
Details	binding site for residue MG B 606

Chain	Residue
B	GLN494
C	LYS497
C	HOH1168
C	HOH1252

site_id	AD5
Number of Residues	5
Details	binding site for residue CA B 607

Chain	Residue
B	HOH763
B	ASP429
B	ASN456
B	THR458
B	TPP602

site_id	AD6
Number of Residues	2
Details	binding site for residue CA B 608

Chain	Residue
B	ASP188
C	ARG185

site_id	AD7
Number of Residues	7
Details	binding site for residue BCT C 601

Chain	Residue
A	HIS282
A	LEU462
A	PHE465
A	TPP602
C	SER27
C	HIS71
C	LEU111

site_id	AD8
Number of Residues	23
Details	binding site for residue TPP C 602

Chain	Residue
A	ASN24
A	PRO25
A	GLY26
A	GLU48
A	HIS71
A	ASN78
A	BCT601
C	THR378
C	SER379
C	GLY402
C	LEU404
C	GLY428
C	ASP429
C	GLY430
C	SER431
C	TYR434
C	ASN456
C	THR458
C	TYR459
C	GLY460
C	ALA461
C	CA603
C	HOH761

site_id	AD9
Number of Residues	5
Details	binding site for residue CA C 603

Chain	Residue
C	ASP429
C	ASN456
C	THR458
C	TPP602
C	HOH743

site_id	AE1
Number of Residues	7
Details	binding site for residue BCT D 601

Chain	Residue
B	HIS282
B	LEU462
B	TPP602
B	HOH1091
D	SER27
D	HIS71
D	LEU111

site_id	AE2
Number of Residues	23
Details	binding site for residue TPP D 602

Chain	Residue
B	ASN24
B	PRO25
B	GLY26
B	GLU48
B	HIS71
B	ASN78
B	BCT601
D	THR378
D	SER379
D	GLY402
D	LEU404
D	GLY428
D	ASP429
D	GLY430
D	SER431
D	TYR434
D	ASN456
D	THR458
D	TYR459
D	GLY460
D	ALA461
D	CA604
D	HOH779

site_id	AE3
Number of Residues	2
Details	binding site for residue MG D 603

Chain	Residue
A	GLN494
D	LYS497

site_id	AE4
Number of Residues	5
Details	binding site for residue CA D 604

Chain	Residue
D	ASP429
D	ASN456
D	THR458
D	TPP602
D	HOH749

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE412-SER431

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	332
Details	Region: {"description":"Thiamine pyrophosphate binding"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 220

Chain	Residue	Details
A	GLY26	electrostatic stabiliser, hydrogen bond donor
A	SER27	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
A	GLU29	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLU48	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS71	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	HIS282	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLY402	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA2
Number of Residues	7
Details	M-CSA 220

Chain	Residue	Details
B	GLY26	electrostatic stabiliser, hydrogen bond donor
B	SER27	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
B	GLU29	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLU48	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS71	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	HIS282	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLY402	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA3
Number of Residues	7
Details	M-CSA 220

Chain	Residue	Details
C	GLY26	electrostatic stabiliser, hydrogen bond donor
C	SER27	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
C	GLU29	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	GLU48	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	HIS71	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	HIS282	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	GLY402	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA4
Number of Residues	7
Details	M-CSA 220

Chain	Residue	Details
D	GLY26	electrostatic stabiliser, hydrogen bond donor
D	SER27	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
D	GLU29	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	GLU48	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	HIS71	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	HIS282	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	GLY402	electrostatic stabiliser, hydrogen bond acceptor

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