Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1NKQ

Crystal structure of yeast ynq8, a fumarylacetoacetate hydrolase family protein

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003674	molecular_function	molecular_function
A	0003824	molecular_function	catalytic activity
A	0005739	cellular_component	mitochondrion
A	0006107	biological_process	oxaloacetate metabolic process
A	0008150	biological_process	biological_process
A	0016853	molecular_function	isomerase activity
A	0018773	molecular_function	acetylpyruvate hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0050163	molecular_function	oxaloacetate tautomerase activity
B	0003674	molecular_function	molecular_function
B	0003824	molecular_function	catalytic activity
B	0005739	cellular_component	mitochondrion
B	0006107	biological_process	oxaloacetate metabolic process
B	0008150	biological_process	biological_process
B	0016853	molecular_function	isomerase activity
B	0018773	molecular_function	acetylpyruvate hydrolase activity
B	0046872	molecular_function	metal ion binding
B	0050163	molecular_function	oxaloacetate tautomerase activity
C	0003674	molecular_function	molecular_function
C	0003824	molecular_function	catalytic activity
C	0005739	cellular_component	mitochondrion
C	0006107	biological_process	oxaloacetate metabolic process
C	0008150	biological_process	biological_process
C	0016853	molecular_function	isomerase activity
C	0018773	molecular_function	acetylpyruvate hydrolase activity
C	0046872	molecular_function	metal ion binding
C	0050163	molecular_function	oxaloacetate tautomerase activity
D	0003674	molecular_function	molecular_function
D	0003824	molecular_function	catalytic activity
D	0005739	cellular_component	mitochondrion
D	0006107	biological_process	oxaloacetate metabolic process
D	0008150	biological_process	biological_process
D	0016853	molecular_function	isomerase activity
D	0018773	molecular_function	acetylpyruvate hydrolase activity
D	0046872	molecular_function	metal ion binding
D	0050163	molecular_function	oxaloacetate tautomerase activity
E	0003674	molecular_function	molecular_function
E	0003824	molecular_function	catalytic activity
E	0005739	cellular_component	mitochondrion
E	0006107	biological_process	oxaloacetate metabolic process
E	0008150	biological_process	biological_process
E	0016853	molecular_function	isomerase activity
E	0018773	molecular_function	acetylpyruvate hydrolase activity
E	0046872	molecular_function	metal ion binding
E	0050163	molecular_function	oxaloacetate tautomerase activity
F	0003674	molecular_function	molecular_function
F	0003824	molecular_function	catalytic activity
F	0005739	cellular_component	mitochondrion
F	0006107	biological_process	oxaloacetate metabolic process
F	0008150	biological_process	biological_process
F	0016853	molecular_function	isomerase activity
F	0018773	molecular_function	acetylpyruvate hydrolase activity
F	0046872	molecular_function	metal ion binding
F	0050163	molecular_function	oxaloacetate tautomerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 260

Chain	Residue
A	GLU87
A	GLU89
A	ASP121
A	ACY701
A	HOH833

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 800

Chain	Residue
B	PRO437
B	TRP438
B	THR439
B	HOH872
A	PHE37
A	PRO137
A	TRP138
A	THR139

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 801

Chain	Residue
A	ARG80
A	GLY81
A	ARG257
A	HOH883
A	HOH905
D	ARG310
D	HIS397
D	PRO508
D	HOH819

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 803

Chain	Residue
A	HIS22
A	ILE23
C	HIS22
C	ILE23

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 560

Chain	Residue
B	GLU387
B	GLU389
B	ASP421
B	ACY703
B	HOH854

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 B 802

Chain	Residue
B	ARG380
B	GLY381
B	ARG557
B	HOH814
B	HOH859
B	HOH892
B	HOH908
F	ARG310
F	HIS397
F	PRO508

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 805

Chain	Residue
B	HIS322
B	ILE323
B	HOH836
B	HOH858
E	HIS22
E	ILE23

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 260

Chain	Residue
C	GLU87
C	GLU89
C	ASP121
C	ACY705
C	HOH867

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 C 806

Chain	Residue
C	PRO137
C	TRP138
C	THR139
C	HOH839
D	PRO437
D	TRP438
D	THR439
D	HOH817

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 560

Chain	Residue
D	GLU387
D	GLU389
D	ASP421
D	ACY707
D	HOH784

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 260

Chain	Residue
E	GLU87
E	GLU89
E	ASP121
E	ACY709
E	HOH882

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 E 807

Chain	Residue
E	PRO137
E	TRP138
E	THR139
E	HOH907
F	PRO437
F	TRP438
F	THR439

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA F 560

Chain	Residue
F	GLU387
F	GLU389
F	ASP421
F	ACY711
F	HOH789

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY A 700

Chain	Residue
A	ARG17
A	GLN128
A	LYS132
A	TRP138

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY A 701

Chain	Residue
A	ILE15
A	GLY16
A	ARG17
A	GLU87
A	GLU89
A	CA260

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACY B 702

Chain	Residue
B	ARG317
B	LYS432

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY B 703

Chain	Residue
B	ARG317
B	GLU387
B	GLU389
B	CA560

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY C 704

Chain	Residue
C	GLN128
C	LYS132
C	TRP138
C	ACY705
C	ARG17

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY C 705

Chain	Residue
C	GLY16
C	ARG17
C	GLU87
C	CA260
C	ACY704

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACY D 706

Chain	Residue
D	ARG317
D	LYS432
D	ACY707

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACY D 707

Chain	Residue
D	ARG317
D	GLU387
D	THR516
D	CA560
D	ACY706

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY E 708

Chain	Residue
E	ARG17
E	GLN128
E	LYS132
E	TRP138

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACY E 709

Chain	Residue
E	ILE15
E	GLY16
E	ARG17
E	PHE37
E	GLU87
E	CA260

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACY F 710

Chain	Residue
F	ARG317
F	ARG425
F	LYS432

site_id	CC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ACY F 711

Chain	Residue
F	ILE315
F	GLY316
F	ARG317
F	PHE337
F	GLU387
F	GLU389
F	LYS442
F	CA560
F	HOH731

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q6P587","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)