Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6SBJ

X-ray structure of mus musculus Fumarylacetoacetate hydrolase domain containing protein 1 (FAHD1) apo-form uuncomplexed

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005654	cellular_component	nucleoplasm
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0005759	cellular_component	mitochondrial matrix
A	0005829	cellular_component	cytosol
A	0006107	biological_process	oxaloacetate metabolic process
A	0008948	molecular_function	oxaloacetate decarboxylase activity
A	0016787	molecular_function	hydrolase activity
A	0016829	molecular_function	lyase activity
A	0016853	molecular_function	isomerase activity
A	0018773	molecular_function	acetylpyruvate hydrolase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0034545	molecular_function	fumarylpyruvate hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0047621	molecular_function	acylpyruvate hydrolase activity
A	0050163	molecular_function	oxaloacetate tautomerase activity
B	0003824	molecular_function	catalytic activity
B	0005654	cellular_component	nucleoplasm
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0005759	cellular_component	mitochondrial matrix
B	0005829	cellular_component	cytosol
B	0006107	biological_process	oxaloacetate metabolic process
B	0008948	molecular_function	oxaloacetate decarboxylase activity
B	0016787	molecular_function	hydrolase activity
B	0016829	molecular_function	lyase activity
B	0016853	molecular_function	isomerase activity
B	0018773	molecular_function	acetylpyruvate hydrolase activity
B	0019752	biological_process	carboxylic acid metabolic process
B	0034545	molecular_function	fumarylpyruvate hydrolase activity
B	0046872	molecular_function	metal ion binding
B	0047621	molecular_function	acylpyruvate hydrolase activity
B	0050163	molecular_function	oxaloacetate tautomerase activity
C	0003824	molecular_function	catalytic activity
C	0005654	cellular_component	nucleoplasm
C	0005739	cellular_component	mitochondrion
C	0005743	cellular_component	mitochondrial inner membrane
C	0005759	cellular_component	mitochondrial matrix
C	0005829	cellular_component	cytosol
C	0006107	biological_process	oxaloacetate metabolic process
C	0008948	molecular_function	oxaloacetate decarboxylase activity
C	0016787	molecular_function	hydrolase activity
C	0016829	molecular_function	lyase activity
C	0016853	molecular_function	isomerase activity
C	0018773	molecular_function	acetylpyruvate hydrolase activity
C	0019752	biological_process	carboxylic acid metabolic process
C	0034545	molecular_function	fumarylpyruvate hydrolase activity
C	0046872	molecular_function	metal ion binding
C	0047621	molecular_function	acylpyruvate hydrolase activity
C	0050163	molecular_function	oxaloacetate tautomerase activity
D	0003824	molecular_function	catalytic activity
D	0005654	cellular_component	nucleoplasm
D	0005739	cellular_component	mitochondrion
D	0005743	cellular_component	mitochondrial inner membrane
D	0005759	cellular_component	mitochondrial matrix
D	0005829	cellular_component	cytosol
D	0006107	biological_process	oxaloacetate metabolic process
D	0008948	molecular_function	oxaloacetate decarboxylase activity
D	0016787	molecular_function	hydrolase activity
D	0016829	molecular_function	lyase activity
D	0016853	molecular_function	isomerase activity
D	0018773	molecular_function	acetylpyruvate hydrolase activity
D	0019752	biological_process	carboxylic acid metabolic process
D	0034545	molecular_function	fumarylpyruvate hydrolase activity
D	0046872	molecular_function	metal ion binding
D	0047621	molecular_function	acylpyruvate hydrolase activity
D	0050163	molecular_function	oxaloacetate tautomerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue MG A 301

Chain	Residue
A	LYS21
A	ASN22
A	HOH403
B	LYS21
B	ASN22
B	HOH423

site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 302

Chain	Residue
A	HOH402
A	HOH408
A	HOH422
A	GLU74
A	GLU76
A	ASP105

site_id	AC3
Number of Residues	6
Details	binding site for residue CL A 303

Chain	Residue
A	CYS68
A	ARG69
A	ASN70
A	ALA108
A	ASP110
A	VAL111

site_id	AC4
Number of Residues	4
Details	binding site for residue CL A 304

Chain	Residue
A	PRO121
A	TRP122
B	PRO121
B	TRP122

site_id	AC5
Number of Residues	7
Details	binding site for residue MG B 301

Chain	Residue
B	GLU74
B	GLU76
B	ASP105
B	LYS126
B	HOH410
B	HOH422
B	HOH436

site_id	AC6
Number of Residues	7
Details	binding site for residue CL B 302

Chain	Residue
B	CYS68
B	ARG69
B	ASN70
B	ALA108
B	ARG109
B	ASP110
B	VAL111

site_id	AC7
Number of Residues	5
Details	binding site for residue MG C 301

Chain	Residue
C	GLU74
C	GLU76
C	ASP105
C	HOH402
C	HOH412

site_id	AC8
Number of Residues	3
Details	binding site for residue CL C 302

Chain	Residue
C	TRP122
D	PRO121
D	TRP122

site_id	AC9
Number of Residues	5
Details	binding site for residue CL C 303

Chain	Residue
C	ARG69
C	ASN70
C	ALA108
C	ASP110
C	VAL111

site_id	AD1
Number of Residues	6
Details	binding site for residue MG D 301

Chain	Residue
C	LYS21
C	ASN22
C	HOH408
D	LYS21
D	ASN22
D	HOH407

site_id	AD2
Number of Residues	6
Details	binding site for residue MG D 302

Chain	Residue
D	VAL26
D	GLU74
D	GLU76
D	ASP105
D	HOH401
D	HOH419

site_id	AD3
Number of Residues	5
Details	binding site for residue CL D 303

Chain	Residue
D	CYS68
D	ARG69
D	ASN70
D	ALA108
D	ASP110

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32068790","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6SBI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32068790","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6SBI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6SBJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q6AYQ8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23576753","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	23
Details	Transit peptide: {"description":"Mitochondrion","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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