Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1F8M

CRYSTAL STRUCTURE OF 3-BROMOPYRUVATE MODIFIED ISOCITRATE LYASE (ICL) FROM MYCOBACTERIUM TUBERCULOSIS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004451	molecular_function	isocitrate lyase activity
A	0005576	cellular_component	extracellular region
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006097	biological_process	glyoxylate cycle
A	0006099	biological_process	tricarboxylic acid cycle
A	0006102	biological_process	isocitrate metabolic process
A	0016829	molecular_function	lyase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0035375	molecular_function	zymogen binding
A	0046421	molecular_function	methylisocitrate lyase activity
A	0046872	molecular_function	metal ion binding
A	0071456	biological_process	cellular response to hypoxia
B	0003824	molecular_function	catalytic activity
B	0004451	molecular_function	isocitrate lyase activity
B	0005576	cellular_component	extracellular region
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006097	biological_process	glyoxylate cycle
B	0006099	biological_process	tricarboxylic acid cycle
B	0006102	biological_process	isocitrate metabolic process
B	0016829	molecular_function	lyase activity
B	0019752	biological_process	carboxylic acid metabolic process
B	0035375	molecular_function	zymogen binding
B	0046421	molecular_function	methylisocitrate lyase activity
B	0046872	molecular_function	metal ion binding
B	0071456	biological_process	cellular response to hypoxia
C	0003824	molecular_function	catalytic activity
C	0004451	molecular_function	isocitrate lyase activity
C	0005576	cellular_component	extracellular region
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006097	biological_process	glyoxylate cycle
C	0006099	biological_process	tricarboxylic acid cycle
C	0006102	biological_process	isocitrate metabolic process
C	0016829	molecular_function	lyase activity
C	0019752	biological_process	carboxylic acid metabolic process
C	0035375	molecular_function	zymogen binding
C	0046421	molecular_function	methylisocitrate lyase activity
C	0046872	molecular_function	metal ion binding
C	0071456	biological_process	cellular response to hypoxia
D	0003824	molecular_function	catalytic activity
D	0004451	molecular_function	isocitrate lyase activity
D	0005576	cellular_component	extracellular region
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006097	biological_process	glyoxylate cycle
D	0006099	biological_process	tricarboxylic acid cycle
D	0006102	biological_process	isocitrate metabolic process
D	0016829	molecular_function	lyase activity
D	0019752	biological_process	carboxylic acid metabolic process
D	0035375	molecular_function	zymogen binding
D	0046421	molecular_function	methylisocitrate lyase activity
D	0046872	molecular_function	metal ion binding
D	0071456	biological_process	cellular response to hypoxia

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 451

Chain	Residue
A	ASP153
A	HOH1148
A	HOH1188
A	HOH2011

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 452

Chain	Residue
B	ASP153
B	HOH1046
B	HOH1499
B	HOH2001
B	HOH2015

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 453

Chain	Residue
C	ASP153
C	HOH1138
C	HOH1454
C	HOH1473
C	HOH2016

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 454

Chain	Residue
D	ASP153
D	HOH1199
D	HOH1299
D	HOH1336
D	HOH1999

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PYR A 500

Chain	Residue
A	TRP93
A	ASP108
A	CYS191
A	HIS193
A	ASN313
A	SER315
A	SER317
A	THR347
A	HOH1409

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PYR B 500

Chain	Residue
B	TRP93
B	ASP108
B	CYS191
B	GLY192
B	HIS193
B	ASN313
B	SER315
B	SER317
B	THR347
B	HOH1352
B	HOH1465

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PYR C 500

Chain	Residue
C	TRP93
C	ASP108
C	CYS191
C	HIS193
C	ASN313
C	SER315
C	SER317
C	THR347
C	HOH1714

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PYR D 500

Chain	Residue
D	ASP108
D	CYS191
D	GLY192
D	HIS193
D	ASN313
D	SER315
D	SER317
D	THR347
D	HOH1290
D	HOH1299

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LYS189-LEU194

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000305\|PubMed:24354272

Chain	Residue	Details
A	LYS190
B	LYS190
C	LYS190
D	LYS190

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:10932251

Chain	Residue	Details
A	LEU90
B	ALA227
B	TYR312
B	ILE346
C	LEU90
C	ALA152
C	CYS191
C	ALA227
C	TYR312
C	ILE346
D	LEU90
A	ALA152
D	ALA152
D	CYS191
D	ALA227
D	TYR312
D	ILE346
A	CYS191
A	ALA227
A	TYR312
A	ILE346
B	LEU90
B	ALA152
B	CYS191

site_id	SWS_FT_FI3
Number of Residues	8
Details	CROSSLNK: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) => ECO:0000269\|PubMed:20066036

Chain	Residue	Details
A	GLN333
B	GLN333
C	GLN333
D	GLN333

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 10932251

Chain	Residue	Details
A	CYS191
A	HIS193
A	ARG228
A	HIS180

site_id	MCSA1
Number of Residues	7
Details	M-CSA 272

Chain	Residue	Details
A	ASP153	metal ligand
A	HIS180	electrostatic stabiliser, hydrogen bond donor
A	CYS191	covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base)
A	HIS193	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base)
A	ARG228	electrostatic stabiliser, hydrogen bond donor
A	SER315	electrostatic stabiliser, hydrogen bond donor
A	SER317	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	7
Details	M-CSA 272

Chain	Residue	Details
B	ASP153	metal ligand
B	HIS180	electrostatic stabiliser, hydrogen bond donor
B	CYS191	covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base)
B	HIS193	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base)
B	ARG228	electrostatic stabiliser, hydrogen bond donor
B	SER315	electrostatic stabiliser, hydrogen bond donor
B	SER317	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	7
Details	M-CSA 272

Chain	Residue	Details
C	ASP153	metal ligand
C	HIS180	electrostatic stabiliser, hydrogen bond donor
C	CYS191	covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base)
C	HIS193	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base)
C	ARG228	electrostatic stabiliser, hydrogen bond donor
C	SER315	electrostatic stabiliser, hydrogen bond donor
C	SER317	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	7
Details	M-CSA 272

Chain	Residue	Details
D	ASP153	metal ligand
D	HIS180	electrostatic stabiliser, hydrogen bond donor
D	CYS191	covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base)
D	HIS193	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base)
D	ARG228	electrostatic stabiliser, hydrogen bond donor
D	SER315	electrostatic stabiliser, hydrogen bond donor
D	SER317	electrostatic stabiliser, hydrogen bond donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)