Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4M8D

Crystal structure of an isatin hydrolase bound to product analogue thioisatinate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004061	molecular_function	arylformamidase activity
A	0016787	molecular_function	hydrolase activity
A	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A	0019441	biological_process	tryptophan catabolic process to kynurenine
A	0030145	molecular_function	manganese ion binding
A	0046872	molecular_function	metal ion binding
B	0004061	molecular_function	arylformamidase activity
B	0016787	molecular_function	hydrolase activity
B	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
B	0019441	biological_process	tryptophan catabolic process to kynurenine
B	0030145	molecular_function	manganese ion binding
B	0046872	molecular_function	metal ion binding
C	0004061	molecular_function	arylformamidase activity
C	0016787	molecular_function	hydrolase activity
C	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
C	0019441	biological_process	tryptophan catabolic process to kynurenine
C	0030145	molecular_function	manganese ion binding
C	0046872	molecular_function	metal ion binding
D	0004061	molecular_function	arylformamidase activity
D	0016787	molecular_function	hydrolase activity
D	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
D	0019441	biological_process	tryptophan catabolic process to kynurenine
D	0030145	molecular_function	manganese ion binding
D	0046872	molecular_function	metal ion binding
E	0004061	molecular_function	arylformamidase activity
E	0016787	molecular_function	hydrolase activity
E	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
E	0019441	biological_process	tryptophan catabolic process to kynurenine
E	0030145	molecular_function	manganese ion binding
E	0046872	molecular_function	metal ion binding
F	0004061	molecular_function	arylformamidase activity
F	0016787	molecular_function	hydrolase activity
F	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
F	0019441	biological_process	tryptophan catabolic process to kynurenine
F	0030145	molecular_function	manganese ion binding
F	0046872	molecular_function	metal ion binding
G	0004061	molecular_function	arylformamidase activity
G	0016787	molecular_function	hydrolase activity
G	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
G	0019441	biological_process	tryptophan catabolic process to kynurenine
G	0030145	molecular_function	manganese ion binding
G	0046872	molecular_function	metal ion binding
H	0004061	molecular_function	arylformamidase activity
H	0016787	molecular_function	hydrolase activity
H	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
H	0019441	biological_process	tryptophan catabolic process to kynurenine
H	0030145	molecular_function	manganese ion binding
H	0046872	molecular_function	metal ion binding
I	0004061	molecular_function	arylformamidase activity
I	0016787	molecular_function	hydrolase activity
I	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
I	0019441	biological_process	tryptophan catabolic process to kynurenine
I	0030145	molecular_function	manganese ion binding
I	0046872	molecular_function	metal ion binding
J	0004061	molecular_function	arylformamidase activity
J	0016787	molecular_function	hydrolase activity
J	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
J	0019441	biological_process	tryptophan catabolic process to kynurenine
J	0030145	molecular_function	manganese ion binding
J	0046872	molecular_function	metal ion binding
K	0004061	molecular_function	arylformamidase activity
K	0016787	molecular_function	hydrolase activity
K	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
K	0019441	biological_process	tryptophan catabolic process to kynurenine
K	0030145	molecular_function	manganese ion binding
K	0046872	molecular_function	metal ion binding
L	0004061	molecular_function	arylformamidase activity
L	0016787	molecular_function	hydrolase activity
L	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
L	0019441	biological_process	tryptophan catabolic process to kynurenine
L	0030145	molecular_function	manganese ion binding
L	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 301

Chain	Residue
A	HIS73
A	HIS77
A	ASP79
A	23J302
A	HOH717

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 23J A 302

Chain	Residue
A	HIS83
A	GLY196
A	PHE209
A	HIS212
A	MN301
A	HOH438
A	HOH502
A	HOH717
A	LEU35
A	HIS73
A	HIS77
A	ASP79

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA A 303

Chain	Residue
A	HOH716
F	HOH517

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 304

Chain	Residue
A	HOH416
A	HOH423
A	HOH431
A	HOH432
A	HOH480
B	HOH444
B	HOH496

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA A 305

Chain	Residue
A	ASN228
A	HOH627
A	HOH654

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN B 301

Chain	Residue
B	HIS73
B	HIS77
B	ASP79
B	23J302
B	HOH460

site_id	AC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 23J B 302

Chain	Residue
A	PHE63
A	TRP65
B	LEU35
B	LEU37
B	PHE41
B	HIS73
B	HIS77
B	ASP79
B	HIS83
B	GLY196
B	PHE209
B	HIS212
B	MN301
B	HOH436
B	HOH437
B	HOH460

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 303

Chain	Residue
B	GLY156
B	HOH570
B	HOH653
C	HOH521
C	HOH543
C	HOH632

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 304

Chain	Residue
B	GLN201
B	HOH407
B	HOH519
K	GLN201
K	HOH411
K	HOH439

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 305

Chain	Residue
B	ASN228
B	ASP230
B	HOH717
B	HOH720

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 301

Chain	Residue
C	HIS73
C	HIS77
C	ASP79
C	23J302
C	HOH637

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 23J C 302

Chain	Residue
C	LEU35
C	HIS73
C	HIS77
C	ASP79
C	HIS83
C	HIS212
C	MN301
C	HOH469
C	HOH637
D	PHE63
D	TRP65

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 303

Chain	Residue
C	GLN201
C	HOH416
C	HOH446
C	HOH547
H	GLN201
H	HOH421

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 304

Chain	Residue
C	ASN228
C	ASP230
C	LYS231
C	HOH474
C	HOH602

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN D 301

Chain	Residue
D	HIS73
D	HIS77
D	ASP79
D	23J302
D	HOH530

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 23J D 302

Chain	Residue
D	LEU35
D	HIS73
D	HIS77
D	ASP79
D	HIS83
D	GLY196
D	HIS212
D	MN301
D	HOH447
D	HOH530
C	TRP65

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 303

Chain	Residue
B	HOH667
D	ASN228
D	HOH484
D	HOH592
D	HOH616

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN E 301

Chain	Residue
E	HIS73
E	HIS77
E	ASP79
E	23J302
E	HOH472

site_id	CC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 23J E 302

Chain	Residue
E	LEU35
E	HIS73
E	HIS77
E	ASP79
E	HIS83
E	GLY196
E	HIS212
E	MN301
E	HOH472
E	HOH665
F	PHE63

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN F 301

Chain	Residue
F	HIS73
F	HIS77
F	ASP79
F	23J302
F	HOH498

site_id	CC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 23J F 302

Chain	Residue
E	PHE63
E	TRP65
F	LEU35
F	LEU37
F	HIS73
F	HIS77
F	ASP79
F	HIS83
F	GLY196
F	PHE209
F	HIS212
F	MN301
F	HOH498
F	HOH719

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA F 303

Chain	Residue
A	GLN201
A	HOH533
F	GLN201
F	HOH408
F	HOH415
F	HOH495

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN G 301

Chain	Residue
G	HIS73
G	HIS77
G	ASP79
G	23J302
G	HOH465

site_id	CC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 23J G 302

Chain	Residue
G	LEU35
G	LEU37
G	PHE41
G	HIS73
G	HIS77
G	ASP79
G	HIS83
G	TRP84
G	GLY196
G	PHE209
G	HIS212
G	MN301
G	HOH441
G	HOH454
G	HOH465
H	PHE63

site_id	CC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN H 301

Chain	Residue
H	HIS73
H	HIS77
H	ASP79
H	23J302
H	HOH635

site_id	CC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 23J H 302

Chain	Residue
G	PHE63
H	LEU35
H	HIS73
H	HIS77
H	ASP79
H	HIS83
H	GLY196
H	PHE209
H	HIS212
H	MN301
H	HOH451
H	HOH635
H	HOH636

site_id	CC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN I 301

Chain	Residue
I	HIS73
I	HIS77
I	ASP79
I	23J302
I	HOH482

site_id	DC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 23J I 302

Chain	Residue
I	LEU35
I	HIS73
I	HIS77
I	ASP79
I	HIS83
I	GLY196
I	HIS212
I	MN301
I	HOH482
I	HOH681
J	PHE63
J	TRP65

site_id	DC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA I 303

Chain	Residue
D	GLN201
I	GLN201
I	HOH401
I	HOH402
I	HOH419
I	HOH497

site_id	DC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN J 301

Chain	Residue
J	HIS73
J	HIS77
J	ASP79
J	23J302
J	HOH433

site_id	DC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 23J J 302

Chain	Residue
I	PHE63
J	LEU35
J	HIS73
J	HIS77
J	ASP79
J	HIS83
J	GLY196
J	PHE209
J	HIS212
J	MN301
J	HOH433
J	HOH447
J	HOH658

site_id	DC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA J 303

Chain	Residue
J	GLN201
J	HOH407
J	HOH419
J	HOH496
J	HOH511

site_id	DC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA J 304

Chain	Residue
J	ASN228
J	HOH454
J	HOH564
J	HOH597

site_id	DC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN K 301

Chain	Residue
K	HIS73
K	HIS77
K	ASP79
K	23J302
K	HOH448

site_id	DC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 23J K 302

Chain	Residue
K	LEU35
K	HIS73
K	HIS77
K	ASP79
K	HIS83
K	GLY196
K	HIS212
K	MN301
K	HOH448
K	HOH679
L	PHE63

site_id	DC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN L 301

Chain	Residue
L	HIS73
L	HIS77
L	ASP79
L	23J302
L	HOH455

site_id	EC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 23J L 302

Chain	Residue
L	LEU35
L	HIS73
L	HIS77
L	ASP79
L	HIS83
L	GLY196
L	PHE209
L	HIS212
L	MN301
L	HOH447
L	HOH455
L	HOH675

site_id	EC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA L 303

Chain	Residue
L	GLN201
L	HOH411
L	HOH415
L	HOH434
L	HOH549

site_id	EC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA L 304

Chain	Residue
L	HOH501
L	HOH552
L	HOH636
L	HOH673
L	HOH674

site_id	EC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA L 305

Chain	Residue
L	ASN228
L	HOH446
L	HOH540
L	HOH584
L	HOH599
L	HOH615

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305\|PubMed:24917679

Chain	Residue	Details
A	HIS83
J	HIS83
K	HIS83
L	HIS83
B	HIS83
C	HIS83
D	HIS83
E	HIS83
F	HIS83
G	HIS83
H	HIS83
I	HIS83

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000305\|PubMed:24917679

Chain	Residue	Details
A	PHE62
J	PHE62
K	PHE62
L	PHE62
B	PHE62
C	PHE62
D	PHE62
E	PHE62
F	PHE62
G	PHE62
H	PHE62
I	PHE62

site_id	SWS_FT_FI3
Number of Residues	36
Details	BINDING: BINDING => ECO:0000269\|PubMed:24917679, ECO:0007744\|PDB:4J0N, ECO:0007744\|PDB:4M8D

Chain	Residue	Details
A	HIS73
D	HIS73
D	HIS77
D	ASP79
E	HIS73
E	HIS77
E	ASP79
F	HIS73
F	HIS77
F	ASP79
G	HIS73
A	HIS77
G	HIS77
G	ASP79
H	HIS73
H	HIS77
H	ASP79
I	HIS73
I	HIS77
I	ASP79
J	HIS73
J	HIS77
A	ASP79
J	ASP79
K	HIS73
K	HIS77
K	ASP79
L	HIS73
L	HIS77
L	ASP79
B	HIS73
B	HIS77
B	ASP79
C	HIS73
C	HIS77
C	ASP79

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:24917679, ECO:0007744\|PDB:4M8D

Chain	Residue	Details
A	HIS212
J	HIS212
K	HIS212
L	HIS212
B	HIS212
C	HIS212
D	HIS212
E	HIS212
F	HIS212
G	HIS212
H	HIS212
I	HIS212

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