Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6FOG

X-ray structure of homo sapiens Fumarylacetoacetate hydrolase domain containing protein 1 (FAHD1) in complex with inhibitor oxalate at 1.94A resolution.

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	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	0018773	molecular_function	acetylpyruvate hydrolase activity
A	0034545	molecular_function	fumarylpyruvate hydrolase activity
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	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	0018773	molecular_function	acetylpyruvate hydrolase activity
B	0034545	molecular_function	fumarylpyruvate hydrolase activity
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	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	0018773	molecular_function	acetylpyruvate hydrolase activity
C	0034545	molecular_function	fumarylpyruvate hydrolase activity
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	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	0018773	molecular_function	acetylpyruvate hydrolase activity
D	0034545	molecular_function	fumarylpyruvate hydrolase activity
D	0047621	molecular_function	acylpyruvate hydrolase activity
D	0050163	molecular_function	oxaloacetate tautomerase activity
E	0003824	molecular_function	catalytic activity
E	0005654	cellular_component	nucleoplasm
E	0005739	cellular_component	mitochondrion
E	0005759	cellular_component	mitochondrial matrix
E	0005829	cellular_component	cytosol
E	0006107	biological_process	oxaloacetate metabolic process
E	0008948	molecular_function	oxaloacetate decarboxylase activity
E	0018773	molecular_function	acetylpyruvate hydrolase activity
E	0034545	molecular_function	fumarylpyruvate hydrolase activity
E	0047621	molecular_function	acylpyruvate hydrolase activity
E	0050163	molecular_function	oxaloacetate tautomerase activity
F	0003824	molecular_function	catalytic activity
F	0005654	cellular_component	nucleoplasm
F	0005739	cellular_component	mitochondrion
F	0005759	cellular_component	mitochondrial matrix
F	0005829	cellular_component	cytosol
F	0006107	biological_process	oxaloacetate metabolic process
F	0008948	molecular_function	oxaloacetate decarboxylase activity
F	0018773	molecular_function	acetylpyruvate hydrolase activity
F	0034545	molecular_function	fumarylpyruvate hydrolase activity
F	0047621	molecular_function	acylpyruvate hydrolase activity
F	0050163	molecular_function	oxaloacetate tautomerase activity
G	0003824	molecular_function	catalytic activity
G	0005654	cellular_component	nucleoplasm
G	0005739	cellular_component	mitochondrion
G	0005759	cellular_component	mitochondrial matrix
G	0005829	cellular_component	cytosol
G	0006107	biological_process	oxaloacetate metabolic process
G	0008948	molecular_function	oxaloacetate decarboxylase activity
G	0018773	molecular_function	acetylpyruvate hydrolase activity
G	0034545	molecular_function	fumarylpyruvate hydrolase activity
G	0047621	molecular_function	acylpyruvate hydrolase activity
G	0050163	molecular_function	oxaloacetate tautomerase activity
H	0003824	molecular_function	catalytic activity
H	0005654	cellular_component	nucleoplasm
H	0005739	cellular_component	mitochondrion
H	0005759	cellular_component	mitochondrial matrix
H	0005829	cellular_component	cytosol
H	0006107	biological_process	oxaloacetate metabolic process
H	0008948	molecular_function	oxaloacetate decarboxylase activity
H	0018773	molecular_function	acetylpyruvate hydrolase activity
H	0034545	molecular_function	fumarylpyruvate hydrolase activity
H	0047621	molecular_function	acylpyruvate hydrolase activity
H	0050163	molecular_function	oxaloacetate tautomerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 301

Chain	Residue
A	GLU71
A	GLU73
A	ASP102
A	OXL302
A	HOH411

site_id	AC2
Number of Residues	12
Details	binding site for residue OXL A 302

Chain	Residue
A	GLU71
A	GLU73
A	ASP102
A	LYS123
A	GLY191
A	THR192
A	MG301
A	HOH418
A	VAL23
A	GLY24
A	ARG25
A	HIS30

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

Chain	Residue
A	TRP119
C	PRO118
C	TRP119

site_id	AC4
Number of Residues	6
Details	binding site for residue MG G 301

Chain	Residue
G	GLU71
G	GLU73
G	ASP102
G	LYS123
G	OXL302
G	HOH404

site_id	AC5
Number of Residues	14
Details	binding site for residue OXL G 302

Chain	Residue
G	VAL23
G	GLY24
G	ARG25
G	HIS30
G	PHE45
G	GLU71
G	GLU73
G	ASP102
G	LYS123
G	GLY191
G	THR192
G	MG301
G	HOH404
G	HOH413

site_id	AC6
Number of Residues	5
Details	binding site for residue MG F 301

Chain	Residue
F	GLU71
F	GLU73
F	ASP102
F	OXL303
F	HOH407

site_id	AC7
Number of Residues	6
Details	binding site for residue MG F 302

Chain	Residue
F	LYS18
F	ASN19
F	HOH420
H	LYS18
H	ASN19
H	HOH432

site_id	AC8
Number of Residues	14
Details	binding site for residue OXL F 303

Chain	Residue
F	VAL23
F	GLY24
F	ARG25
F	HIS30
F	PHE45
F	GLU71
F	GLU73
F	ASP102
F	LYS123
F	GLY191
F	THR192
F	MG301
F	HOH416
F	HOH430

site_id	AC9
Number of Residues	3
Details	binding site for residue CL F 304

Chain	Residue
F	TRP119
H	PRO118
H	TRP119

site_id	AD1
Number of Residues	5
Details	binding site for residue MG D 301

Chain	Residue
D	GLU71
D	GLU73
D	ASP102
D	OXL303
D	HOH430

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

Chain	Residue
B	LYS18
B	ASN19
B	HOH450
D	LYS18
D	ASN19
D	HOH437

site_id	AD3
Number of Residues	12
Details	binding site for residue OXL D 303

Chain	Residue
D	GLY24
D	ARG25
D	HIS30
D	GLU71
D	GLU73
D	ASP102
D	LYS123
D	GLY191
D	THR192
D	MG301
D	HOH443
D	HOH454

site_id	AD4
Number of Residues	5
Details	binding site for residue MG B 301

Chain	Residue
B	GLU71
B	GLU73
B	ASP102
B	OXL302
B	HOH411

site_id	AD5
Number of Residues	15
Details	binding site for residue OXL B 302

Chain	Residue
B	PHE45
B	GLU71
B	GLU73
B	ASP102
B	LYS123
B	GLY191
B	THR192
B	MG301
B	HOH402
B	HOH411
B	HOH418
B	HOH447
B	GLY24
B	ARG25
B	HIS30

site_id	AD6
Number of Residues	3
Details	binding site for residue CL B 303

Chain	Residue
B	TRP119
D	PRO118
D	TRP119

site_id	AD7
Number of Residues	6
Details	binding site for residue MG A 304

Chain	Residue
A	LYS18
A	ASN19
A	HOH447
C	LYS18
C	ASN19
C	HOH433

site_id	AD8
Number of Residues	5
Details	binding site for residue MG C 301

Chain	Residue
C	GLU71
C	GLU73
C	ASP102
C	OXL302
C	HOH422

site_id	AD9
Number of Residues	15
Details	binding site for residue OXL C 302

Chain	Residue
C	VAL23
C	GLY24
C	ARG25
C	HIS30
C	PHE45
C	GLU71
C	GLU73
C	ASP102
C	LYS123
C	GLY191
C	THR192
C	MG301
C	HOH414
C	HOH423
C	HOH428

site_id	AE1
Number of Residues	5
Details	binding site for residue MG H 301

Chain	Residue
H	GLU71
H	GLU73
H	ASP102
H	OXL302
H	HOH402

site_id	AE2
Number of Residues	15
Details	binding site for residue OXL H 302

Chain	Residue
H	VAL23
H	GLY24
H	ARG25
H	HIS30
H	PHE45
H	GLU71
H	GLU73
H	ASP102
H	LYS123
H	GLY191
H	THR192
H	MG301
H	HOH402
H	HOH429
H	HOH442

site_id	AE3
Number of Residues	5
Details	binding site for residue MG E 301

Chain	Residue
E	GLU71
E	GLU73
E	ASP102
E	OXL302
E	HOH423

site_id	AE4
Number of Residues	6
Details	binding site for residue MG G 303

Chain	Residue
E	LYS18
E	ASN19
E	HOH415
G	LYS18
G	ASN19
G	HOH458

site_id	AE5
Number of Residues	14
Details	binding site for residue OXL E 302

Chain	Residue
E	VAL23
E	GLY24
E	ARG25
E	HIS30
E	PHE45
E	GLU71
E	GLU73
E	ASP102
E	LYS123
E	GLY191
E	THR192
E	MG301
E	HOH417
E	HOH423

site_id	AE6
Number of Residues	3
Details	binding site for residue CL E 303

Chain	Residue
E	TRP119
E	HOH431
G	TRP119

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30348641","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6FOG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15551868","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30348641","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SAW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6FOG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6FOH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q6AYQ8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8R0F8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8R0F8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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