Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4APB

Crystal structure of Mycobacterium tuberculosis fumarase (Rv1098c) S318C in complex with fumarate

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	12
Details	BINDING SITE FOR RESIDUE FUM A 1469

Chain	Residue
A	CYS318
C	ASN140
D	THR186
D	HIS187
A	SER319
A	ILE320
A	MET321
A	LYS324
A	ASN326
C	THR106
C	SER138
C	SER139

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 1470

Chain	Residue
A	SER256
A	HOH2296
A	HOH2297
A	HOH2302

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE FUM B 1469

Chain	Residue
B	CYS318
B	SER319
B	ILE320
B	MET321
B	LYS324
B	ASN326
C	THR186
C	HIS187
D	THR106
D	SER138
D	SER139
D	ASN140

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 1470

Chain	Residue
B	GLY124
B	HOH2121
B	HOH2181
B	HOH2182
D	HOH2372

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE FUM C 1469

Chain	Residue
A	THR106
A	SER138
A	SER139
A	ASN140
B	THR186
B	HIS187
C	GLY317
C	CYS318
C	SER319
C	ILE320
C	MET321
C	LYS324
C	ASN326

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE FUM D 1471

Chain	Residue
A	THR186
A	HIS187
B	THR106
B	SER138
B	SER139
B	ASN140
D	CYS318
D	SER319
D	MET321
D	LYS324
D	ASN326

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA D 1472

Chain	Residue
D	SER256
D	HOH2253
D	HOH2254
D	HOH2256
D	HOH2258
D	HOH2382
D	HOH2383

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	CYS318
B	CYS318
C	CYS318
D	CYS318

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)