Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4JUB

Crystal Structure of the His70Thr mutant of 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	0016831	molecular_function	carboxy-lyase activity
A	0018924	biological_process	mandelate metabolic process
A	0019439	biological_process	obsolete aromatic compound catabolic 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	0016831	molecular_function	carboxy-lyase activity
B	0018924	biological_process	mandelate metabolic process
B	0019439	biological_process	obsolete aromatic compound catabolic 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	0016831	molecular_function	carboxy-lyase activity
C	0018924	biological_process	mandelate metabolic process
C	0019439	biological_process	obsolete aromatic compound catabolic 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	0016831	molecular_function	carboxy-lyase activity
D	0018924	biological_process	mandelate metabolic process
D	0019439	biological_process	obsolete aromatic compound catabolic 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 MG A 601

Chain	Residue
A	ASN117
A	LEU118
A	ARG120
D	ASN117
D	LEU118
D	ARG120

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 602

Chain	Residue
A	TPP603
A	HOH713
A	ASP428
A	ASN455
A	THR457

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE TPP A 603

Chain	Residue
A	GLU375
A	THR377
A	SER378
A	GLY401
A	LEU403
A	GLY427
A	ASP428
A	GLY429
A	SER430
A	TYR433
A	THR457
A	TYR458
A	GLY459
A	ALA460
A	LEU461
A	CA602
A	HOH740
D	ASN23
D	PRO24
D	GLY25
D	GLU47
D	THR70
D	ASN77

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 604

Chain	Residue
A	GLN421
A	LEU511
A	HOH753
A	HOH772
A	HOH781
A	HOH813
C	GLU419

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 605

Chain	Residue
A	ARG101
A	GLU128
A	PRO129
A	ALA130
C	ARG101
C	GLU128
C	PRO129
C	ALA130

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 601

Chain	Residue
B	ASN117
B	LEU118
B	ARG120
C	ASN117
C	LEU118
C	ARG120

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 602

Chain	Residue
B	ASP428
B	ASN455
B	THR457
B	TPP603
B	HOH704

site_id	AC8
Number of Residues	23
Details	BINDING SITE FOR RESIDUE TPP B 603

Chain	Residue
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	CA602
B	HOH737
C	ASN23
C	PRO24
C	GLY25
C	GLU47
C	THR70
C	ASN77

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 601

Chain	Residue
C	ASP428
C	ASN455
C	THR457
C	TPP602
C	HOH707

site_id	BC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE TPP C 602

Chain	Residue
C	GLY427
C	ASP428
C	GLY429
C	SER430
C	TYR433
C	ASN455
C	THR457
C	TYR458
C	GLY459
C	ALA460
C	CA601
C	HOH720
B	ASN23
B	PRO24
B	GLY25
B	GLU47
B	THR70
B	ASN77
C	GLU375
C	THR377
C	SER378
C	GLY401
C	LEU403

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 601

Chain	Residue
D	ASP428
D	ASN455
D	THR457
D	TPP602
D	HOH706

site_id	BC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE TPP D 602

Chain	Residue
A	ASN23
A	PRO24
A	GLY25
A	GLU47
A	THR70
A	ASN77
D	GLU375
D	THR377
D	SER378
D	GLY401
D	LEU403
D	GLY427
D	ASP428
D	GLY429
D	SER430
D	TYR433
D	THR457
D	TYR458
D	GLY459
D	ALA460
D	LEU461
D	CA601
D	HOH756

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	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	THR70	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	THR70	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	THR70	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	THR70	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)