Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6SBI

X-ray structure of murine Fumarylacetoacetate hydrolase domain containing protein 1 (FAHD1) in complex with inhibitor oxalate

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	GLU74
A	GLU76
A	ASP105
A	LYS126
A	OXL306
A	HOH404

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

Chain	Residue
B	LYS21
B	ASN22
B	HOH412
A	LYS21
A	ASN22
A	HOH402

site_id	AC3
Number of Residues	3
Details	binding site for residue CL A 303

Chain	Residue
A	PRO121
A	TRP122
B	TRP122

site_id	AC4
Number of Residues	6
Details	binding site for residue CL A 304

Chain	Residue
A	ARG69
A	ASN70
A	ALA108
A	ARG109
A	ASP110
A	VAL111

site_id	AC5
Number of Residues	1
Details	binding site for residue CL A 305

Chain	Residue
A	GLU207

site_id	AC6
Number of Residues	13
Details	binding site for residue OXL A 306

Chain	Residue
A	GLY27
A	ARG28
A	HIS33
A	PHE48
A	GLU74
A	GLU76
A	ASP105
A	LYS126
A	GLY194
A	THR195
A	MG301
A	HOH404
A	HOH405

site_id	AC7
Number of Residues	6
Details	binding site for residue MG B 301

Chain	Residue
B	GLU74
B	GLU76
B	ASP105
B	LYS126
B	OXL304
B	HOH405

site_id	AC8
Number of Residues	4
Details	binding site for residue CL B 302

Chain	Residue
B	CYS68
B	ARG69
B	ASN70
B	ALA108

site_id	AC9
Number of Residues	6
Details	binding site for residue CL B 303

Chain	Residue
B	HIS147
B	ALA148
B	LEU149
B	LYS164
B	THR165
B	SER166

site_id	AD1
Number of Residues	12
Details	binding site for residue OXL B 304

Chain	Residue
B	VAL26
B	GLY27
B	ARG28
B	HIS33
B	GLU74
B	GLU76
B	ASP105
B	LYS126
B	GLY194
B	THR195
B	MG301
B	HOH405

site_id	AD2
Number of Residues	6
Details	binding site for residue MG C 301

Chain	Residue
C	GLU74
C	GLU76
C	ASP105
C	LYS126
C	OXL306
C	HOH401

site_id	AD3
Number of Residues	6
Details	binding site for residue K C 302

Chain	Residue
C	LYS21
C	ASN22
C	HOH405
D	LYS21
D	ASN22
D	HOH404

site_id	AD4
Number of Residues	6
Details	binding site for residue CL C 303

Chain	Residue
C	ARG69
C	ASN70
C	ALA108
C	ARG109
C	ASP110
C	VAL111

site_id	AD5
Number of Residues	1
Details	binding site for residue CL C 304

Chain	Residue
C	GLU58

site_id	AD6
Number of Residues	3
Details	binding site for residue CL C 305

Chain	Residue
C	PRO121
C	TRP122
D	TRP122

site_id	AD7
Number of Residues	11
Details	binding site for residue OXL C 306

Chain	Residue
C	GLY27
C	ARG28
C	HIS33
C	GLU74
C	GLU76
C	ASP105
C	LYS126
C	GLY194
C	THR195
C	MG301
C	HOH401

site_id	AD8
Number of Residues	6
Details	binding site for residue MG D 301

Chain	Residue
D	LYS126
D	OXL303
D	HOH403
D	GLU74
D	GLU76
D	ASP105

site_id	AD9
Number of Residues	5
Details	binding site for residue CL D 302

Chain	Residue
D	ARG69
D	ASN70
D	ALA108
D	ASP110
D	VAL111

site_id	AE1
Number of Residues	11
Details	binding site for residue OXL D 303

Chain	Residue
D	GLY27
D	ARG28
D	HIS33
D	GLU74
D	GLU76
D	ASP105
D	LYS126
D	GLY194
D	THR195
D	MG301
D	HOH403

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

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