Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6UNZ

Crystal structure of cytosolic fumarate hydratase from Leishmania major

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004333	molecular_function	fumarate hydratase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006091	biological_process	generation of precursor metabolites and energy
A	0006106	biological_process	fumarate metabolic process
A	0006108	biological_process	malate metabolic process
A	0016829	molecular_function	lyase activity
A	0016836	molecular_function	hydro-lyase activity
A	0020015	cellular_component	glycosome
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	0097014	cellular_component	ciliary plasm
B	0004333	molecular_function	fumarate hydratase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006091	biological_process	generation of precursor metabolites and energy
B	0006106	biological_process	fumarate metabolic process
B	0006108	biological_process	malate metabolic process
B	0016829	molecular_function	lyase activity
B	0016836	molecular_function	hydro-lyase activity
B	0020015	cellular_component	glycosome
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0097014	cellular_component	ciliary plasm
C	0004333	molecular_function	fumarate hydratase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006091	biological_process	generation of precursor metabolites and energy
C	0006106	biological_process	fumarate metabolic process
C	0006108	biological_process	malate metabolic process
C	0016829	molecular_function	lyase activity
C	0016836	molecular_function	hydro-lyase activity
C	0020015	cellular_component	glycosome
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
C	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0097014	cellular_component	ciliary plasm
D	0004333	molecular_function	fumarate hydratase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006091	biological_process	generation of precursor metabolites and energy
D	0006106	biological_process	fumarate metabolic process
D	0006108	biological_process	malate metabolic process
D	0016829	molecular_function	lyase activity
D	0016836	molecular_function	hydro-lyase activity
D	0020015	cellular_component	glycosome
D	0042803	molecular_function	protein homodimerization activity
D	0046872	molecular_function	metal ion binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding
D	0097014	cellular_component	ciliary plasm
E	0004333	molecular_function	fumarate hydratase activity
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006091	biological_process	generation of precursor metabolites and energy
E	0006106	biological_process	fumarate metabolic process
E	0006108	biological_process	malate metabolic process
E	0016829	molecular_function	lyase activity
E	0016836	molecular_function	hydro-lyase activity
E	0020015	cellular_component	glycosome
E	0042803	molecular_function	protein homodimerization activity
E	0046872	molecular_function	metal ion binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
E	0097014	cellular_component	ciliary plasm
F	0004333	molecular_function	fumarate hydratase activity
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006091	biological_process	generation of precursor metabolites and energy
F	0006106	biological_process	fumarate metabolic process
F	0006108	biological_process	malate metabolic process
F	0016829	molecular_function	lyase activity
F	0016836	molecular_function	hydro-lyase activity
F	0020015	cellular_component	glycosome
F	0042803	molecular_function	protein homodimerization activity
F	0046872	molecular_function	metal ion binding
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding
F	0097014	cellular_component	ciliary plasm
G	0004333	molecular_function	fumarate hydratase activity
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006091	biological_process	generation of precursor metabolites and energy
G	0006106	biological_process	fumarate metabolic process
G	0006108	biological_process	malate metabolic process
G	0016829	molecular_function	lyase activity
G	0016836	molecular_function	hydro-lyase activity
G	0020015	cellular_component	glycosome
G	0042803	molecular_function	protein homodimerization activity
G	0046872	molecular_function	metal ion binding
G	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	0097014	cellular_component	ciliary plasm
H	0004333	molecular_function	fumarate hydratase activity
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0006091	biological_process	generation of precursor metabolites and energy
H	0006106	biological_process	fumarate metabolic process
H	0006108	biological_process	malate metabolic process
H	0016829	molecular_function	lyase activity
H	0016836	molecular_function	hydro-lyase activity
H	0020015	cellular_component	glycosome
H	0042803	molecular_function	protein homodimerization activity
H	0046872	molecular_function	metal ion binding
H	0051539	molecular_function	4 iron, 4 sulfur cluster binding
H	0097014	cellular_component	ciliary plasm

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue SF4 A 601

Chain	Residue
A	CYS133
A	LYS491
A	GLN134
A	ASP135
A	GLY214
A	ALA251
A	CYS252
A	CYS346
A	ALA348
A	ARG350

site_id	AC2
Number of Residues	9
Details	binding site for residue SF4 B 601

Chain	Residue
B	CYS133
B	GLN134
B	ASP135
B	GLY214
B	ALA251
B	CYS252
B	CYS346
B	ALA348
B	ARG350

site_id	AC3
Number of Residues	7
Details	binding site for residue GOL B 602

Chain	Residue
A	HIS334
A	ALA336
B	GLN134
B	ARG173
B	ARG421
B	THR467
B	LYS491

site_id	AC4
Number of Residues	9
Details	binding site for residue SF4 C 601

Chain	Residue
C	CYS133
C	GLN134
C	GLY214
C	ALA251
C	CYS252
C	CYS346
C	SER347
C	ALA348
C	LYS491

site_id	AC5
Number of Residues	9
Details	binding site for residue SF4 D 601

Chain	Residue
D	CYS133
D	GLN134
D	ASP135
D	GLY216
D	SER217
D	CYS252
D	CYS346
D	SER347
D	ALA348

site_id	AC6
Number of Residues	8
Details	binding site for residue SF4 E 601

Chain	Residue
E	CYS133
E	ALA251
E	CYS252
E	CYS346
E	ALA348
E	ARG350
E	LYS491
E	GOL602

site_id	AC7
Number of Residues	7
Details	binding site for residue GOL E 602

Chain	Residue
E	ASP135
E	ARG173
E	ARG421
E	PRO466
E	THR467
E	LYS491
E	SF4601

site_id	AC8
Number of Residues	9
Details	binding site for residue SF4 F 601

Chain	Residue
F	CYS133
F	GLN134
F	ASP135
F	GLY214
F	SER217
F	CYS252
F	CYS346
F	SER347
F	ALA348

site_id	AC9
Number of Residues	4
Details	binding site for residue SF4 G 601

Chain	Residue
G	CYS133
G	ASP135
G	CYS252
G	CYS346

site_id	AD1
Number of Residues	11
Details	binding site for residue SF4 H 601

Chain	Residue
H	CYS133
H	GLN134
H	ASP135
H	GLY214
H	GLY216
H	SER217
H	ALA251
H	CYS252
H	CYS346
H	SER347
H	ALA348

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	80
Details	BINDING: BINDING => ECO:0000269\|PubMed:27528683, ECO:0007744\|PDB:5L2R

Chain	Residue	Details
A	CYS133
A	LYS491
B	CYS133
B	GLN134
B	ARG173
B	GLY216
B	ASN219
B	CYS252
B	CYS346
B	ARG421
B	THR467
A	GLN134
B	LYS491
C	CYS133
C	GLN134
C	ARG173
C	GLY216
C	ASN219
C	CYS252
C	CYS346
C	ARG421
C	THR467
A	ARG173
C	LYS491
D	CYS133
D	GLN134
D	ARG173
D	GLY216
D	ASN219
D	CYS252
D	CYS346
D	ARG421
D	THR467
A	GLY216
D	LYS491
E	CYS133
E	GLN134
E	ARG173
E	GLY216
E	ASN219
E	CYS252
E	CYS346
E	ARG421
E	THR467
A	ASN219
E	LYS491
F	CYS133
F	GLN134
F	ARG173
F	GLY216
F	ASN219
F	CYS252
F	CYS346
F	ARG421
F	THR467
A	CYS252
F	LYS491
G	CYS133
G	GLN134
G	ARG173
G	GLY216
G	ASN219
G	CYS252
G	CYS346
G	ARG421
G	THR467
A	CYS346
G	LYS491
H	CYS133
H	GLN134
H	ARG173
H	GLY216
H	ASN219
H	CYS252
H	CYS346
H	ARG421
H	THR467
A	ARG421
H	LYS491
A	THR467

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