Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1MCZ

BENZOYLFORMATE DECARBOXYLASE FROM PSEUDOMONAS PUTIDA COMPLEXED WITH AN INHIBITOR, R-MANDELATE

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
E	0000287	molecular_function	magnesium ion binding
E	0003824	molecular_function	catalytic activity
E	0003984	molecular_function	acetolactate synthase activity
E	0016829	molecular_function	lyase activity
E	0016831	molecular_function	carboxy-lyase activity
E	0018924	biological_process	mandelate metabolic process
E	0019596	biological_process	mandelate catabolic process
E	0019752	biological_process	carboxylic acid metabolic process
E	0030976	molecular_function	thiamine pyrophosphate binding
E	0046872	molecular_function	metal ion binding
E	0050660	molecular_function	flavin adenine dinucleotide binding
E	0050695	molecular_function	benzoylformate decarboxylase activity
F	0000287	molecular_function	magnesium ion binding
F	0003824	molecular_function	catalytic activity
F	0003984	molecular_function	acetolactate synthase activity
F	0016829	molecular_function	lyase activity
F	0016831	molecular_function	carboxy-lyase activity
F	0018924	biological_process	mandelate metabolic process
F	0019596	biological_process	mandelate catabolic process
F	0019752	biological_process	carboxylic acid metabolic process
F	0030976	molecular_function	thiamine pyrophosphate binding
F	0046872	molecular_function	metal ion binding
F	0050660	molecular_function	flavin adenine dinucleotide binding
F	0050695	molecular_function	benzoylformate decarboxylase activity
G	0000287	molecular_function	magnesium ion binding
G	0003824	molecular_function	catalytic activity
G	0003984	molecular_function	acetolactate synthase activity
G	0016829	molecular_function	lyase activity
G	0016831	molecular_function	carboxy-lyase activity
G	0018924	biological_process	mandelate metabolic process
G	0019596	biological_process	mandelate catabolic process
G	0019752	biological_process	carboxylic acid metabolic process
G	0030976	molecular_function	thiamine pyrophosphate binding
G	0046872	molecular_function	metal ion binding
G	0050660	molecular_function	flavin adenine dinucleotide binding
G	0050695	molecular_function	benzoylformate decarboxylase activity
H	0000287	molecular_function	magnesium ion binding
H	0003824	molecular_function	catalytic activity
H	0003984	molecular_function	acetolactate synthase activity
H	0016829	molecular_function	lyase activity
H	0016831	molecular_function	carboxy-lyase activity
H	0018924	biological_process	mandelate metabolic process
H	0019596	biological_process	mandelate catabolic process
H	0019752	biological_process	carboxylic acid metabolic process
H	0030976	molecular_function	thiamine pyrophosphate binding
H	0046872	molecular_function	metal ion binding
H	0050660	molecular_function	flavin adenine dinucleotide binding
H	0050695	molecular_function	benzoylformate decarboxylase activity
I	0000287	molecular_function	magnesium ion binding
I	0003824	molecular_function	catalytic activity
I	0003984	molecular_function	acetolactate synthase activity
I	0016829	molecular_function	lyase activity
I	0016831	molecular_function	carboxy-lyase activity
I	0018924	biological_process	mandelate metabolic process
I	0019596	biological_process	mandelate catabolic process
I	0019752	biological_process	carboxylic acid metabolic process
I	0030976	molecular_function	thiamine pyrophosphate binding
I	0046872	molecular_function	metal ion binding
I	0050660	molecular_function	flavin adenine dinucleotide binding
I	0050695	molecular_function	benzoylformate decarboxylase activity
J	0000287	molecular_function	magnesium ion binding
J	0003824	molecular_function	catalytic activity
J	0003984	molecular_function	acetolactate synthase activity
J	0016829	molecular_function	lyase activity
J	0016831	molecular_function	carboxy-lyase activity
J	0018924	biological_process	mandelate metabolic process
J	0019596	biological_process	mandelate catabolic process
J	0019752	biological_process	carboxylic acid metabolic process
J	0030976	molecular_function	thiamine pyrophosphate binding
J	0046872	molecular_function	metal ion binding
J	0050660	molecular_function	flavin adenine dinucleotide binding
J	0050695	molecular_function	benzoylformate decarboxylase activity
K	0000287	molecular_function	magnesium ion binding
K	0003824	molecular_function	catalytic activity
K	0003984	molecular_function	acetolactate synthase activity
K	0016829	molecular_function	lyase activity
K	0016831	molecular_function	carboxy-lyase activity
K	0018924	biological_process	mandelate metabolic process
K	0019596	biological_process	mandelate catabolic process
K	0019752	biological_process	carboxylic acid metabolic process
K	0030976	molecular_function	thiamine pyrophosphate binding
K	0046872	molecular_function	metal ion binding
K	0050660	molecular_function	flavin adenine dinucleotide binding
K	0050695	molecular_function	benzoylformate decarboxylase activity
L	0000287	molecular_function	magnesium ion binding
L	0003824	molecular_function	catalytic activity
L	0003984	molecular_function	acetolactate synthase activity
L	0016829	molecular_function	lyase activity
L	0016831	molecular_function	carboxy-lyase activity
L	0018924	biological_process	mandelate metabolic process
L	0019596	biological_process	mandelate catabolic process
L	0019752	biological_process	carboxylic acid metabolic process
L	0030976	molecular_function	thiamine pyrophosphate binding
L	0046872	molecular_function	metal ion binding
L	0050660	molecular_function	flavin adenine dinucleotide binding
L	0050695	molecular_function	benzoylformate decarboxylase activity
M	0000287	molecular_function	magnesium ion binding
M	0003824	molecular_function	catalytic activity
M	0003984	molecular_function	acetolactate synthase activity
M	0016829	molecular_function	lyase activity
M	0016831	molecular_function	carboxy-lyase activity
M	0018924	biological_process	mandelate metabolic process
M	0019596	biological_process	mandelate catabolic process
M	0019752	biological_process	carboxylic acid metabolic process
M	0030976	molecular_function	thiamine pyrophosphate binding
M	0046872	molecular_function	metal ion binding
M	0050660	molecular_function	flavin adenine dinucleotide binding
M	0050695	molecular_function	benzoylformate decarboxylase activity
N	0000287	molecular_function	magnesium ion binding
N	0003824	molecular_function	catalytic activity
N	0003984	molecular_function	acetolactate synthase activity
N	0016829	molecular_function	lyase activity
N	0016831	molecular_function	carboxy-lyase activity
N	0018924	biological_process	mandelate metabolic process
N	0019596	biological_process	mandelate catabolic process
N	0019752	biological_process	carboxylic acid metabolic process
N	0030976	molecular_function	thiamine pyrophosphate binding
N	0046872	molecular_function	metal ion binding
N	0050660	molecular_function	flavin adenine dinucleotide binding
N	0050695	molecular_function	benzoylformate decarboxylase activity
O	0000287	molecular_function	magnesium ion binding
O	0003824	molecular_function	catalytic activity
O	0003984	molecular_function	acetolactate synthase activity
O	0016829	molecular_function	lyase activity
O	0016831	molecular_function	carboxy-lyase activity
O	0018924	biological_process	mandelate metabolic process
O	0019596	biological_process	mandelate catabolic process
O	0019752	biological_process	carboxylic acid metabolic process
O	0030976	molecular_function	thiamine pyrophosphate binding
O	0046872	molecular_function	metal ion binding
O	0050660	molecular_function	flavin adenine dinucleotide binding
O	0050695	molecular_function	benzoylformate decarboxylase activity
P	0000287	molecular_function	magnesium ion binding
P	0003824	molecular_function	catalytic activity
P	0003984	molecular_function	acetolactate synthase activity
P	0016829	molecular_function	lyase activity
P	0016831	molecular_function	carboxy-lyase activity
P	0018924	biological_process	mandelate metabolic process
P	0019596	biological_process	mandelate catabolic process
P	0019752	biological_process	carboxylic acid metabolic process
P	0030976	molecular_function	thiamine pyrophosphate binding
P	0046872	molecular_function	metal ion binding
P	0050660	molecular_function	flavin adenine dinucleotide binding
P	0050695	molecular_function	benzoylformate decarboxylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 529

Chain	Residue
A	ASP428
A	ASN455
A	THR457
A	TPP533
A	HOH547

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 530

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

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 529

Chain	Residue
B	ASP428
B	ASN455
B	THR457
B	TPP533
B	HOH551

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 529

Chain	Residue
C	ASP428
C	ASN455
C	THR457
C	TPP533
C	HOH550

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 529

Chain	Residue
D	ASP428
D	ASN455
D	THR457
D	TPP533
D	HOH553

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 530

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

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 529

Chain	Residue
E	ASP428
E	ASN455
E	THR457
E	TPP533
E	HOH546

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 530

Chain	Residue
E	ASN117
E	LEU118
E	ARG120
F	ASN117
F	LEU118
F	ARG120

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 529

Chain	Residue
F	ASP428
F	ASN455
F	THR457
F	TPP533
F	HOH554

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG G 529

Chain	Residue
G	ASP428
G	ASN455
G	THR457
G	TPP533
G	HOH550

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG H 529

Chain	Residue
H	ASP428
H	ASN455
H	THR457
H	TPP533
H	HOH553

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG H 530

Chain	Residue
G	ASN117
G	LEU118
G	ARG120
H	LEU118
H	ARG120

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG I 529

Chain	Residue
I	ASP428
I	ASN455
I	THR457
I	TPP533
I	HOH841

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG I 530

Chain	Residue
I	ASN117
I	LEU118
I	ARG120
J	ASN117
J	LEU118
J	ARG120

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG J 529

Chain	Residue
J	ASP428
J	ASN455
J	THR457
J	TPP533
J	HOH945

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG K 529

Chain	Residue
K	ASP428
K	ASN455
K	THR457
K	TPP533
K	HOH549

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG L 529

Chain	Residue
L	ASP428
L	ASN455
L	THR457
L	TPP533
L	HOH557

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG L 530

Chain	Residue
K	ASN117
K	LEU118
K	ARG120
L	ASN117
L	LEU118
L	ARG120

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG M 529

Chain	Residue
M	HOH1255
M	ASP428
M	ASN455
M	THR457
M	TPP533

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG N 529

Chain	Residue
N	ASP428
N	ASN455
N	THR457
N	TPP533
N	HOH552

site_id	CC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG N 530

Chain	Residue
M	ASN117
N	ASN117

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG O 529

Chain	Residue
O	ASP428
O	ASN455
O	THR457
O	TPP533
O	HOH1462

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG P 529

Chain	Residue
P	ASP428
P	ASN455
P	THR457
P	TPP533
P	HOH1566

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG P 530

Chain	Residue
O	LEU118
P	MET79
P	LEU118
P	PRO119
P	ARG120

site_id	CC7
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TPP A 533

Chain	Residue
A	GLU375
A	SER376
A	THR377
A	SER378
A	GLY401
A	LEU403
A	GLY427
A	ASP428
A	GLY429
A	SER430
A	TYR433
A	ASN455
A	THR457
A	TYR458
A	GLY459
A	ALA460
A	LEU461
A	MG529
A	RMN534
B	ASN23
B	PRO24
B	GLY25
B	GLU47
B	HIS70
B	ASN77

site_id	CC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE RMN A 534

Chain	Residue
A	HIS281
A	THR377
A	GLY401
A	LEU461
A	PHE464
A	TPP533
A	HOH601
B	GLY25
B	SER26
B	HIS70
B	LEU110

site_id	CC9
Number of Residues	24
Details	BINDING SITE FOR RESIDUE TPP B 533

Chain	Residue
A	ASN23
A	PRO24
A	GLY25
A	GLU47
A	HIS70
A	ASN77
B	GLU375
B	SER376
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	MG529
B	RMN534

site_id	DC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE RMN B 534

Chain	Residue
A	SER26
A	HIS70
A	LEU110
B	HIS281
B	THR377
B	GLY401
B	LEU461
B	TPP533
B	HOH602

site_id	DC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TPP C 533

Chain	Residue
C	GLU375
C	SER376
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	MG529
C	RMN534
D	ASN23
D	PRO24
D	GLY25
D	GLU47
D	HIS70
D	ASN77

site_id	DC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE RMN C 534

Chain	Residue
C	HIS281
C	THR377
C	GLY401
C	LEU461
C	TPP533
C	HOH603
D	SER26
D	HIS70
D	LEU110

site_id	DC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE TPP D 533

Chain	Residue
C	ASN23
C	PRO24
C	GLY25
C	GLU47
C	HIS70
C	ASN77
D	GLU375
D	SER376
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	MG529
D	RMN534
D	HOH575

site_id	DC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE RMN D 534

Chain	Residue
C	SER26
C	HIS70
C	LEU110
D	HIS281
D	THR377
D	GLY401
D	LEU461
D	PHE464
D	TPP533

site_id	DC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TPP E 533

Chain	Residue
E	GLU375
E	SER376
E	THR377
E	SER378
E	GLY401
E	LEU403
E	GLY427
E	ASP428
E	GLY429
E	SER430
E	TYR433
E	ASN455
E	THR457
E	TYR458
E	GLY459
E	ALA460
E	LEU461
E	MG529
E	RMN534
F	ASN23
F	PRO24
F	GLY25
F	GLU47
F	HIS70
F	ASN77

site_id	DC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE RMN E 534

Chain	Residue
E	HIS281
E	THR377
E	GLY401
E	LEU461
E	TPP533
E	HOH599
F	SER26
F	HIS70
F	LEU110

site_id	DC8
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TPP F 533

Chain	Residue
E	ASN23
E	PRO24
E	GLY25
E	GLU47
E	HIS70
E	ASN77
F	GLU375
F	SER376
F	THR377
F	SER378
F	GLY401
F	LEU403
F	GLY427
F	ASP428
F	GLY429
F	SER430
F	TYR433
F	ASN455
F	THR457
F	TYR458
F	GLY459
F	ALA460
F	LEU461
F	MG529
F	RMN534

site_id	DC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE RMN F 534

Chain	Residue
E	SER26
E	HIS70
E	LEU110
F	HIS281
F	THR377
F	GLY401
F	LEU461
F	PHE464
F	TPP533

site_id	EC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TPP G 533

Chain	Residue
G	GLU375
G	SER376
G	THR377
G	SER378
G	GLY401
G	LEU403
G	GLY427
G	ASP428
G	GLY429
G	SER430
G	TYR433
G	ASN455
G	THR457
G	TYR458
G	GLY459
G	ALA460
G	LEU461
G	MG529
G	RMN534
H	ASN23
H	PRO24
H	GLY25
H	GLU47
H	HIS70
H	ASN77

site_id	EC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE RMN G 534

Chain	Residue
G	HIS281
G	THR377
G	GLY401
G	LEU461
G	PHE464
G	TPP533
H	GLY25
H	SER26
H	HIS70
H	LEU110

site_id	EC3
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TPP H 533

Chain	Residue
G	ASN23
G	PRO24
G	GLY25
G	GLU47
G	HIS70
G	ASN77
H	GLU375
H	SER376
H	THR377
H	SER378
H	GLY401
H	LEU403
H	GLY427
H	ASP428
H	GLY429
H	SER430
H	TYR433
H	ASN455
H	THR457
H	TYR458
H	GLY459
H	ALA460
H	MG529
H	RMN534
H	HOH553

site_id	EC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE RMN H 534

Chain	Residue
G	SER26
G	HIS70
G	LEU110
H	HIS281
H	THR377
H	GLY401
H	LEU461
H	TPP533

site_id	EC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TPP I 533

Chain	Residue
I	GLU375
I	SER376
I	THR377
I	SER378
I	GLY401
I	LEU403
I	GLY427
I	ASP428
I	GLY429
I	SER430
I	TYR433
I	ASN455
I	THR457
I	TYR458
I	GLY459
I	ALA460
I	MG529
I	RMN534
I	HOH865
J	ASN23
J	PRO24
J	GLY25
J	GLU47
J	HIS70
J	ASN77

site_id	EC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE RMN I 534

Chain	Residue
I	HIS281
I	THR377
I	GLY401
I	LEU461
I	TPP533
I	HOH899
J	SER26
J	HIS70
J	LEU110

site_id	EC7
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TPP J 533

Chain	Residue
I	ASN23
I	PRO24
I	GLY25
I	GLU47
I	HIS70
I	ASN77
J	GLU375
J	SER376
J	THR377
J	SER378
J	GLY401
J	LEU403
J	GLY427
J	ASP428
J	GLY429
J	SER430
J	TYR433
J	ASN455
J	THR457
J	TYR458
J	GLY459
J	ALA460
J	LEU461
J	MG529
J	RMN534

site_id	EC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE RMN J 534

Chain	Residue
I	SER26
I	HIS70
I	LEU110
J	HIS281
J	THR377
J	GLY401
J	LEU461
J	PHE464
J	TPP533
J	HOH1002

site_id	EC9
Number of Residues	27
Details	BINDING SITE FOR RESIDUE TPP K 533

Chain	Residue
K	GLU375
K	SER376
K	THR377
K	SER378
K	GLY401
K	LEU403
K	GLY427
K	ASP428
K	GLY429
K	SER430
K	TYR433
K	ASN455
K	THR457
K	TYR458
K	GLY459
K	ALA460
K	LEU461
K	MG529
K	RMN534
K	HOH549
K	HOH572
L	ASN23
L	PRO24
L	GLY25
L	GLU47
L	HIS70
L	ASN77

site_id	FC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE RMN K 534

Chain	Residue
K	HIS281
K	THR377
K	GLY401
K	LEU461
K	PHE464
K	TPP533
L	SER26
L	HIS70
L	LEU110

site_id	FC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE TPP L 533

Chain	Residue
K	ASN23
K	PRO24
K	GLY25
K	GLU47
K	HIS70
K	ASN77
L	GLU375
L	SER376
L	THR377
L	SER378
L	GLY401
L	LEU403
L	GLY427
L	ASP428
L	GLY429
L	SER430
L	TYR433
L	ASN455
L	THR457
L	TYR458
L	GLY459
L	ALA460
L	MG529
L	RMN534

site_id	FC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE RMN L 534

Chain	Residue
K	SER26
K	HIS70
K	LEU110
L	HIS281
L	THR377
L	GLY401
L	LEU461
L	TPP533
L	HOH610

site_id	FC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TPP M 533

Chain	Residue
M	GLU375
M	SER376
M	THR377
M	SER378
M	GLY401
M	LEU403
M	GLY427
M	ASP428
M	GLY429
M	SER430
M	TYR433
M	ASN455
M	THR457
M	TYR458
M	GLY459
M	ALA460
M	MG529
M	RMN534
M	HOH1279
N	ASN23
N	PRO24
N	GLY25
N	GLU47
N	HIS70
N	ASN77

site_id	FC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE RMN M 534

Chain	Residue
M	HIS281
M	THR377
M	GLY401
M	LEU461
M	TPP533
N	SER26
N	HIS70
N	LEU110

site_id	FC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TPP N 533

Chain	Residue
M	ASN23
M	PRO24
M	GLY25
M	GLU47
M	HIS70
M	ASN77
N	GLU375
N	SER376
N	THR377
N	SER378
N	GLY401
N	LEU403
N	GLY427
N	ASP428
N	GLY429
N	SER430
N	TYR433
N	ASN455
N	THR457
N	TYR458
N	GLY459
N	ALA460
N	MG529
N	RMN534
N	HOH574

site_id	FC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE RMN N 534

Chain	Residue
M	SER26
M	HIS70
M	LEU110
N	HIS281
N	THR377
N	GLY401
N	LEU461
N	PHE464
N	TPP533

site_id	FC8
Number of Residues	26
Details	BINDING SITE FOR RESIDUE TPP O 533

Chain	Residue
O	GLU375
O	SER376
O	THR377
O	SER378
O	GLY401
O	LEU403
O	GLY427
O	ASP428
O	GLY429
O	SER430
O	TYR433
O	ASN455
O	THR457
O	TYR458
O	GLY459
O	ALA460
O	LEU461
O	MG529
O	RMN534
O	HOH1486
P	ASN23
P	PRO24
P	GLY25
P	GLU47
P	HIS70
P	ASN77

site_id	FC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE RMN O 534

Chain	Residue
O	HIS281
O	THR377
O	GLY401
O	LEU461
O	TPP533
P	SER26
P	HIS70
P	LEU110

site_id	GC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE TPP P 533

Chain	Residue
O	ASN23
O	PRO24
O	GLY25
O	GLU47
O	HIS70
O	ASN77
P	GLU375
P	SER376
P	THR377
P	SER378
P	GLY401
P	LEU403
P	GLY427
P	ASP428
P	GLY429
P	SER430
P	TYR433
P	ASN455
P	THR457
P	TYR458
P	GLY459
P	ALA460
P	LEU461
P	MG529
P	RMN534
P	HOH1590

site_id	GC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE RMN P 534

Chain	Residue
O	SER26
O	HIS70
O	LEU110
P	HIS281
P	THR377
P	GLY401
P	LEU461
P	TPP533

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	1328
Details	Region: {"description":"Thiamine pyrophosphate binding"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	96
Details	Binding site: {}

Chain

Residue

Details

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	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1bfd

Chain	Residue	Details
J	GLU28
J	HIS281
J	HIS70

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1bfd

Chain	Residue	Details
K	GLU28
K	HIS281
K	HIS70

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1bfd

Chain	Residue	Details
L	GLU28
L	HIS281
L	HIS70

site_id	CSA13
Number of Residues	3
Details	Annotated By Reference To The Literature 1bfd

Chain	Residue	Details
M	GLU28
M	HIS281
M	HIS70

site_id	CSA14
Number of Residues	3
Details	Annotated By Reference To The Literature 1bfd

Chain	Residue	Details
N	GLU28
N	HIS281
N	HIS70

site_id	CSA15
Number of Residues	3
Details	Annotated By Reference To The Literature 1bfd

Chain	Residue	Details
O	GLU28
O	HIS281
O	HIS70

site_id	CSA16
Number of Residues	3
Details	Annotated By Reference To The Literature 1bfd

Chain	Residue	Details
P	GLU28
P	HIS281
P	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	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1bfd

Chain	Residue	Details
E	GLU28
E	HIS281
E	HIS70

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1bfd

Chain	Residue	Details
F	GLU28
F	HIS281
F	HIS70

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1bfd

Chain	Residue	Details
G	GLU28
G	HIS281
G	HIS70

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1bfd

Chain	Residue	Details
H	GLU28
H	HIS281
H	HIS70

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1bfd

Chain	Residue	Details
I	GLU28
I	HIS281
I	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	MCSA10
Number of Residues	7
Details	M-CSA 220

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

site_id	MCSA11
Number of Residues	7
Details	M-CSA 220

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

site_id	MCSA12
Number of Residues	7
Details	M-CSA 220

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

site_id	MCSA13
Number of Residues	7
Details	M-CSA 220

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

site_id	MCSA14
Number of Residues	7
Details	M-CSA 220

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

site_id	MCSA15
Number of Residues	7
Details	M-CSA 220

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

site_id	MCSA16
Number of Residues	7
Details	M-CSA 220

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

site_id	MCSA5
Number of Residues	7
Details	M-CSA 220

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

site_id	MCSA6
Number of Residues	7
Details	M-CSA 220

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

site_id	MCSA7
Number of Residues	7
Details	M-CSA 220

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

site_id	MCSA8
Number of Residues	7
Details	M-CSA 220

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

site_id	MCSA9
Number of Residues	7
Details	M-CSA 220

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

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