Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3OQ8

Crystal structure of isocitrate lyase from Brucella melitensis, bound to the product mimic malonate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004451	molecular_function	isocitrate lyase activity
A	0006097	biological_process	glyoxylate cycle
A	0006099	biological_process	tricarboxylic acid cycle
A	0016829	molecular_function	lyase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0046872	molecular_function	metal ion binding
B	0003824	molecular_function	catalytic activity
B	0004451	molecular_function	isocitrate lyase activity
B	0006097	biological_process	glyoxylate cycle
B	0006099	biological_process	tricarboxylic acid cycle
B	0016829	molecular_function	lyase activity
B	0019752	biological_process	carboxylic acid metabolic process
B	0046872	molecular_function	metal ion binding
C	0003824	molecular_function	catalytic activity
C	0004451	molecular_function	isocitrate lyase activity
C	0006097	biological_process	glyoxylate cycle
C	0006099	biological_process	tricarboxylic acid cycle
C	0016829	molecular_function	lyase activity
C	0019752	biological_process	carboxylic acid metabolic process
C	0046872	molecular_function	metal ion binding
D	0003824	molecular_function	catalytic activity
D	0004451	molecular_function	isocitrate lyase activity
D	0006097	biological_process	glyoxylate cycle
D	0006099	biological_process	tricarboxylic acid cycle
D	0016829	molecular_function	lyase activity
D	0019752	biological_process	carboxylic acid metabolic process
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MLA A 440

Chain	Residue
A	ASP101
A	HOH464
A	HOH560
A	CYS185
A	HIS187
A	ASN309
A	SER311
A	SER313
A	THR343
A	LEU344
A	HOH430

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 450

Chain	Residue
A	ALA92
A	ARG116
A	HOH498
A	HOH547
B	ALA92
B	HOH998
B	HOH1141

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 460

Chain	Residue
A	ASP157
D	SER103
D	HOH534
D	HOH917

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 465

Chain	Residue
A	GLY190
A	LYS191
A	ALA228
A	LYS229
A	LEU230
A	HOH534
B	GLU417

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 475

Chain	Residue
A	MET71
A	ARG75
A	ALA124
A	GLU128
A	ARG391
A	GLU392

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 501

Chain	Residue
A	ASP147
A	HOH430
A	HOH464
A	HOH580
A	HOH945
A	HOH949

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MLA B 440

Chain	Residue
B	CYS185
B	HIS187
B	ASN309
B	SER311
B	SER313
B	THR343
B	HOH430
B	HOH431
B	HOH473
B	HOH542

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA B 460

Chain	Residue
B	ASP157
B	HOH1117
B	HOH1118
C	SER103
C	HOH537

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 465

Chain	Residue
A	GLU417
B	GLY189
B	GLY190
B	LYS191
B	ALA227
B	ALA228
B	LYS229
B	LEU230

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 475

Chain	Residue
B	MET71
B	ARG75
B	ILE127
B	GLU128
B	ARG391
B	GLU392

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA B 501

Chain	Residue
B	ASP147
B	HOH430
B	HOH431
B	HOH432
B	HOH434
B	HOH542

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MLA C 440

Chain	Residue
C	ASP101
C	CYS185
C	HIS187
C	ASN309
C	SER311
C	SER313
C	THR343
C	HOH431
C	HOH527
C	HOH550
C	HOH947

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA C 460

Chain	Residue
B	SER103
B	HOH697
B	HOH961
C	ASP157

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 465

Chain	Residue
C	GLY189
C	GLY190
C	LYS191
C	ALA227
C	LYS229
C	LEU230
C	HOH502

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 470

Chain	Residue
C	ASP239
C	LYS258
C	PRO263
C	ARG267
C	HOH437
C	HOH592
C	LEU193

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 475

Chain	Residue
C	MET71
C	ARG75
C	ALA124
C	ILE127
C	GLU128
C	ARG391
C	GLU392

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA C 501

Chain	Residue
C	ASP147
C	HOH431
C	HOH527
C	HOH635
C	HOH946
C	HOH947

site_id	BC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MLA D 440

Chain	Residue
D	CYS185
D	HIS187
D	ASN309
D	SER311
D	SER313
D	THR343
D	LEU344
D	HOH430
D	HOH529
D	HOH919

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 450

Chain	Residue
C	ARG116
C	HOH658
C	HOH878
C	HOH1018
D	ARG116
D	HOH558

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA D 460

Chain	Residue
A	SER103
A	HOH742
A	HOH1146
D	ASP157

site_id	CC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO D 465

Chain	Residue
C	GLU417
D	GLY189
D	GLY190
D	LYS191
D	ALA227
D	ALA228
D	LYS229
D	LEU230

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO D 475

Chain	Residue
D	MET71
D	ARG75
D	ALA124
D	GLU128
D	ARG391
D	GLU392

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA D 501

Chain	Residue
D	ASP147
D	HOH430
D	HOH431
D	HOH448
D	HOH919
D	HOH948

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA C 430

Chain	Residue
C	VAL243
C	HOH580
C	HOH666
C	HOH1093
C	HOH1120
D	HOH1061

Functional Information from PROSITE/UniProt

site_id	PS00161
Number of Residues	6
Details	ISOCITRATE_LYASE Isocitrate lyase signature. KKCGHL

Chain	Residue	Details
A	LYS183-LEU188

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