Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5F91

Fumarate hydratase of Mycobacterium tuberculosis in complex with formate and allosteric modulator (N-(5-(azepan-1-ylsulfonyl)-2-methoxyphenyl)-2-(4-oxo-3,4-dihydrophthalazin-1-yl)acetamide)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004333	molecular_function	fumarate hydratase activity
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006099	biological_process	tricarboxylic acid cycle
A	0006106	biological_process	fumarate metabolic process
A	0009274	cellular_component	peptidoglycan-based cell wall
A	0016829	molecular_function	lyase activity
B	0003824	molecular_function	catalytic activity
B	0004333	molecular_function	fumarate hydratase activity
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006099	biological_process	tricarboxylic acid cycle
B	0006106	biological_process	fumarate metabolic process
B	0009274	cellular_component	peptidoglycan-based cell wall
B	0016829	molecular_function	lyase activity
C	0003824	molecular_function	catalytic activity
C	0004333	molecular_function	fumarate hydratase activity
C	0005576	cellular_component	extracellular region
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006099	biological_process	tricarboxylic acid cycle
C	0006106	biological_process	fumarate metabolic process
C	0009274	cellular_component	peptidoglycan-based cell wall
C	0016829	molecular_function	lyase activity
D	0003824	molecular_function	catalytic activity
D	0004333	molecular_function	fumarate hydratase activity
D	0005576	cellular_component	extracellular region
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006099	biological_process	tricarboxylic acid cycle
D	0006106	biological_process	fumarate metabolic process
D	0009274	cellular_component	peptidoglycan-based cell wall
D	0016829	molecular_function	lyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue 5WJ A 501

Chain	Residue
A	LEU303
C	ASN394
C	HIS397
C	ARG400
C	LEU401
C	ARG432
C	5WJ501
C	HOH607
C	HOH773
A	THR304
A	GLY305
A	LEU429
A	ARG432
A	HOH718
A	HOH844
C	GLY305
C	ALA307

site_id	AC2
Number of Residues	7
Details	binding site for residue FMT B 501

Chain	Residue
B	GLY317
B	SER318
B	MET321
B	LYS324
B	ASN326
C	ASN140
D	THR186

site_id	AC3
Number of Residues	1
Details	binding site for residue CL B 503

Chain	Residue
B	ASP92

site_id	AC4
Number of Residues	1
Details	binding site for residue CL B 504

Chain	Residue
B	ARG259

site_id	AC5
Number of Residues	17
Details	binding site for residue 5WJ C 501

Chain	Residue
A	GLY305
A	ALA307
A	HIS397
A	ARG400
A	LEU401
A	ARG432
A	5WJ501
A	HOH607
A	HOH811
C	LEU303
C	THR304
C	GLY305
C	LEU429
C	ARG432
C	HOH613
C	HOH706
C	HOH748

Functional Information from PROSITE/UniProt

site_id	PS00163
Number of Residues	10
Details	FUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN

Chain	Residue	Details
A	GLY317-ASN326

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_00743, ECO:0000305\|PubMed:22561013, ECO:0007744\|PDB:4ADL, ECO:0007744\|PDB:4ADM

Chain	Residue	Details
A	HIS187
B	HIS187
C	HIS187
D	HIS187

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00743, ECO:0000269\|PubMed:22561013, ECO:0007744\|PDB:4ADM

Chain	Residue	Details
A	SER318
B	SER318
C	SER318
D	SER318

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00743, ECO:0000269\|PubMed:22561013, ECO:0000269\|PubMed:27325754, ECO:0007744\|PDB:4ADL, ECO:0007744\|PDB:4ADM, ECO:0007744\|PDB:4APB, ECO:0007744\|PDB:5F92

Chain	Residue	Details
A	SER104
B	SER104
C	SER104
D	SER104

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: in site B => ECO:0000255\|HAMAP-Rule:MF_00743

Chain	Residue	Details
A	HIS128
B	HIS128
C	HIS128
D	HIS128

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00743, ECO:0000269\|PubMed:22561013, ECO:0000269\|PubMed:27325754, ECO:0007744\|PDB:4ADL, ECO:0007744\|PDB:4ADM, ECO:0007744\|PDB:4APB, ECO:0007744\|PDB:5F91, ECO:0007744\|PDB:5F92

Chain	Residue	Details
A	SER138
A	LYS324
B	SER138
B	LYS324
C	SER138
C	LYS324
D	SER138
D	LYS324

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00743, ECO:0000269\|PubMed:22561013, ECO:0000269\|PubMed:27325754, ECO:0007744\|PDB:4ADL, ECO:0007744\|PDB:4APB, ECO:0007744\|PDB:5F91, ECO:0007744\|PDB:5F92

Chain	Residue	Details
A	THR186
B	THR186
C	THR186
D	THR186

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00743, ECO:0000269\|PubMed:22561013, ECO:0000269\|PubMed:27325754, ECO:0007744\|PDB:4ADL, ECO:0007744\|PDB:4APB, ECO:0007744\|PDB:5F92

Chain	Residue	Details
A	SER319
B	SER319
C	SER319
D	SER319

site_id	SWS_FT_FI8
Number of Residues	4
Details	SITE: Important for catalytic activity => ECO:0000255\|HAMAP-Rule:MF_00743

Chain	Residue	Details
A	GLU331
B	GLU331
C	GLU331
D	GLU331

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: N-acetylalanine => ECO:0007744\|PubMed:21969609

Chain	Residue	Details
A	ALA2
B	ALA2
C	ALA2
D	ALA2

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