Protein profile

PA4470

fumarate hydratase

Genome: NC_002516.2

Gene: fumC1 Structure source: ColabFold

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Amino acids 458

Annotations 6

Features 32

PDB binders 18

Druggability 0.894

Overview

Basic information about this protein and its source genome.

Accession: PA4470
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: fumC1
Status: annotated
Amino acids: 458
Structure source: ColabFold

GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. GO:0006099 A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle. GO:0004333 Catalysis of the reaction: (S)-malate = fumarate + H2O. GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. GO:0045239 Any of the heteromeric enzymes that act in the TCA cycle. GO:0006106 The chemical reactions and pathways involving fumarate, the anion of trans-1,2-ethenedicarboxylic acid, the diastereoisomer of maleate. It is a key intermediate in metabolism and is formed in the TCA cycle from succinate and converted into malate.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 44.096
Human E-value: 8.58e-112
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.894

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
GO:0006099 A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.
GO:0004333 Catalysis of the reaction: (S)-malate = fumarate + H2O.
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0045239 Any of the heteromeric enzymes that act in the TCA cycle.
GO:0006106 The chemical reactions and pathways involving fumarate, the anion of trans-1,2-ethenedicarboxylic acid, the diastereoisomer of maleate. It is a key intermediate in metabolism and is formed in the TCA cycle from succinate and converted into malate.

Sequence Features

Domain/signature hits from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
4	456	Hamap	MF_00743	Fumarate hydratase class II [fumC].
4	456	InterPro	IPR005677	Fumarate hydratase, class II
3	454	PANTHER	PTHR11444	ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE
3	454	InterPro	IPR005677	Fumarate hydratase, class II
2	132	Gene3D	G3DSA:1.10.275.10	-
2	132	InterPro	IPR024083	Fumarase/histidase, N-terminal
133	400	FunFam	G3DSA:1.20.200.10:FF:000001	Fumarate hydratase, mitochondrial
402	454	Pfam	PF10415	Fumarase C C-terminus
402	454	InterPro	IPR018951	Fumarase C, C-terminal
127	149	PRINTS	PR00145	Argininosuccinate lyase family signature
169	189	PRINTS	PR00145	Argininosuccinate lyase family signature
311	327	PRINTS	PR00145	Argininosuccinate lyase family signature
401	456	FunFam	G3DSA:1.10.40.30:FF:000002	Fumarate hydratase class II
5	132	FunFam	G3DSA:1.10.275.10:FF:000001	Fumarate hydratase, mitochondrial
12	336	Pfam	PF00206	Lyase
12	336	InterPro	IPR022761	Fumarate lyase, N-terminal
174	192	PRINTS	PR00149	Fumarate lyase superfamily signature
174	192	InterPro	IPR000362	Fumarate lyase family
265	292	PRINTS	PR00149	Fumarate lyase superfamily signature
265	292	InterPro	IPR000362	Fumarate lyase family
128	146	PRINTS	PR00149	Fumarate lyase superfamily signature
128	146	InterPro	IPR000362	Fumarate lyase family
311	327	PRINTS	PR00149	Fumarate lyase superfamily signature
311	327	InterPro	IPR000362	Fumarate lyase family
311	320	ProSitePatterns	PS00163	Fumarate lyases signature.
311	320	InterPro	IPR020557	Fumarate lyase, conserved site
400	456	Gene3D	G3DSA:1.10.40.30	-
3	454	SUPERFAMILY	SSF48557	L-aspartase-like
3	454	InterPro	IPR008948	L-Aspartase-like
5	453	CDD	cd01362	Fumarase_classII
5	453	InterPro	IPR005677	Fumarate hydratase, class II
133	399	Gene3D	G3DSA:1.20.200.10	Fumarase/aspartase (Central domain)

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

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Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
ColabFold PA4470	ColabFold	—	—	full sequence	—	Viewing

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
3				0.894
10				0.766
12				0.295

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

68 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
5WJ	5F91	P9WN93	470.6 Da LogP 2.68 TPSA 121.5	✓ Ro5	✓ Clean	`COc1ccc(cc1NC(=O)CC2=NNC(=O)c3c2cccc3)S(=O)(=O)…`
APO	7LUB	P07954	169.1 Da LogP -1.42 TPSA 120.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)N)P(=O)(O)O`
FLC	6P3C	P05042	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
FUM	4APB	P9WN93	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)\C(=O)O`
KUE	6S43	P9WN93	484.6 Da LogP 3.07 TPSA 121.5	✓ Ro5	✓ Clean	`COc1ccc(cc1NC(=O)CC2=NNC(=O)c3c2cccc3)S(=O)(=O)…`
KYZ	6S7K	P9WN93	402.4 Da LogP 1.02 TPSA 130.2	✓ Ro5	✓ Clean	`CNS(=O)(=O)c1ccc(c(c1)NC(=O)CC2=NNC(=O)c3c2cccc…`
KZ8	6S7S	P9WN93	464.5 Da LogP 2.91 TPSA 130.2	✓ Ro5	✓ Clean	`COc1ccc(cc1NC(=O)CC2=NNC(=O)c3c2cccc3)S(=O)(=O)…`
KZK	6S7U	P9WN93	441.6 Da LogP 3.92 TPSA 91.5	✓ Ro5	✓ Clean	`COc1ccc(cc1NC(=O)Cc2c[nH]c3c2cccc3)S(=O)(=O)N4C…`
KZN	6S7Z	P9WN93	504.6 Da LogP 2.86 TPSA 121.5	1 viol.	✓ Clean	`COc1ccc(cc1NC(=O)CC2=NNC(=O)c3c2cccc3)S(=O)(=O)…`
KZT	6S7W	P9WN93	453.6 Da LogP 3.99 TPSA 88.6	✓ Ro5	✓ Clean	`COc1ccc(cc1NC(=O)Cc2ccnc3c2cccc3)S(=O)(=O)N4CCC…`
L0K	6S88	P9WN93	518.6 Da LogP 2.90 TPSA 121.5	1 viol.	✓ Clean	`COc1ccc(cc1NC(=O)CC2=NNC(=O)c3c2cccc3)S(=O)(=O)…`
LMR	3RRP	B1MKP6	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)O)C(=O)O`
MLI	3GTD	Q9ZCQ4	102.0 Da LogP -3.12 TPSA 80.3	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(=O)[O-]`
MLT	1FUO	P05042	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
PMA	1FUP	P05042	254.1 Da LogP 0.48 TPSA 149.2	✓ Ro5	✓ Clean	`c1c(c(cc(c1C(=O)O)C(=O)O)C(=O)O)C(=O)O`
SIF	1FUQ	P05042	190.3 Da LogP 1.25 TPSA 74.6	✓ Ro5	✓ Clean	`C[Si](C)(C)C(CC(=O)O)C(=O)O`
SRT	4ADM	P9WN93	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@H](C(=O)O)O)(C(=O)O)O`
TLA	6VBE	P07954	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)O)O)(C(=O)O)O`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC16045828	1.000	456.5 Da LogP 2.29 TPSA 121.5	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)Cc1n[nH]c(=O…`
ZINC16097357	1.000	441.6 Da LogP 3.92 TPSA 91.5	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCCC2)cc1NC(=O)Cc1c[nH]c2c…`
ZINC391925	1.000	254.1 Da LogP 0.48 TPSA 149.2	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)O)c(C(=O)O)cc1C(=O)O`
ZINC8692724	1.000	427.5 Da LogP 3.53 TPSA 91.5	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)Cc1c[nH]c2cc…`
ZINC9712829	1.000	470.6 Da LogP 2.68 TPSA 121.5	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCCC2)cc1NC(=O)Cc1n[nH]c(=…`
ZINC12528738	0.855	441.6 Da LogP 3.92 TPSA 91.5	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)CCc1c[nH]c2c…`
ZINC9633616	0.855	455.6 Da LogP 4.31 TPSA 91.5	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCCC2)cc1NC(=O)CCc1c[nH]c2…`
ZINC15637940	0.852	442.5 Da LogP 2.29 TPSA 94.7	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCN(C)CC2)cc1NC(=O)Cc1c[nH]c…`
ZINC9252907	0.846	470.6 Da LogP 2.68 TPSA 121.5	✓ Ro5	✓ Clean	`CCOc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)Cc1n[nH]c(=…`
ZINC9508900	0.839	429.5 Da LogP 2.38 TPSA 100.7	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCOCC2)cc1NC(=O)Cc1c[nH]c2cc…`
ZINC13014295	0.828	469.6 Da LogP 4.70 TPSA 91.5	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCCC2)cc1NC(=O)CCCc1c[nH]c…`
ZINC14201048	0.825	455.6 Da LogP 4.31 TPSA 91.5	✓ Ro5	✓ Clean	`CC(C)Oc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)Cc1c[nH]…`
ZINC22204540	0.800	446.3 Da LogP 1.11 TPSA 240.9	1 viol.	✓ Clean	`O=C(O)c1cc(C(=O)O)c(C(=O)c2cc(C(=O)O)c(C(=O)O)c…`
ZINC5455545	0.787	411.5 Da LogP 3.83 TPSA 82.3	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)Cc1c[nH]c2ccc…`
ZINC12821278	0.767	399.5 Da LogP 2.84 TPSA 102.5	✓ Ro5	✓ Clean	`O=C(Cc1c[nH]c2ccccc12)Nc1cc(S(=O)(=O)N2CCCC2)cc…`
ZINC12941959	0.766	428.5 Da LogP 1.59 TPSA 132.5	✓ Ro5	✓ Clean	`O=C(Cc1n[nH]c(=O)c2ccccc12)Nc1cc(S(=O)(=O)N2CCC…`
ZINC9703758	0.746	484.6 Da LogP 2.69 TPSA 110.6	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCCC2)cc1NC(=O)Cc1nn(C)c(=…`
ZINC9704140	0.746	470.6 Da LogP 2.30 TPSA 110.6	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)Cc1nn(C)c(=O…`
ZINC13149731	0.746	427.5 Da LogP 3.99 TPSA 91.5	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCCC2)cc1NC(=O)c1c[nH]c2cc…`
ZINC13145325	0.746	388.5 Da LogP 3.05 TPSA 75.7	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)Cc1ccccc1`
ZINC13598250	0.746	402.5 Da LogP 3.44 TPSA 75.7	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCCC2)cc1NC(=O)Cc1ccccc1`
ZINC5558941	0.746	418.5 Da LogP 3.06 TPSA 84.9	✓ Ro5	✓ Clean	`COc1ccccc1CC(=O)Nc1cc(S(=O)(=O)N2CCCCC2)ccc1OC`
ZINC89473611	0.746	432.5 Da LogP 3.45 TPSA 84.9	✓ Ro5	✓ Clean	`COc1ccccc1CC(=O)Nc1cc(S(=O)(=O)N2CCCCCC2)ccc1OC`
ZINC9955279	0.739	497.6 Da LogP 3.13 TPSA 115.5	✓ Ro5	✓ Clean	`CCN(CC)c1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)Cc1n[nH…`
ZINC9338426	0.734	478.5 Da LogP 3.22 TPSA 130.2	✓ Ro5	✓ Clean	`COc1ccccc1NS(=O)(=O)c1ccc(C)c(NC(=O)Cc2n[nH]c(=…`
ZINC9491232	0.727	456.5 Da LogP 2.83 TPSA 110.7	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)COc1ncnc2ccc…`
ZINC32809952	0.723	455.5 Da LogP 3.35 TPSA 108.6	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCCC2)cc1NC(=O)c1c[nH]c2cc…`
ZINC8694034	0.723	427.5 Da LogP 3.53 TPSA 91.5	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)Cc2c[nH]c3ccccc23)cc1S(=O)(=O)N1C…`
ZINC5558939	0.721	422.9 Da LogP 3.70 TPSA 75.7	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)Cc1ccccc1Cl`
ZINC9704103	0.721	437.0 Da LogP 4.09 TPSA 75.7	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCCC2)cc1NC(=O)Cc1ccccc1Cl`
ZINC9492963	0.721	443.5 Da LogP 2.77 TPSA 100.7	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCOCC2)cc1NC(=O)CCc1c[nH]c2c…`
ZINC26738060	0.714	465.5 Da LogP 4.17 TPSA 109.5	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)Nc2ccccc2OC)cc1NC(=O)Cc1c[nH]c…`
ZINC14230122	0.710	469.6 Da LogP 4.70 TPSA 91.5	✓ Ro5	✓ Clean	`CC(C)Oc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)CCc1c[nH…`
ZINC13040018	0.706	470.6 Da LogP 2.61 TPSA 110.6	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCCC2)cc1NC(=O)Cn1cnc2cccc…`
ZINC4289585	0.706	226.1 Da LogP 0.49 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)c1cc(C(=O)O)c(C(=O)O)cc1O`
ZINC4863098	0.706	250.2 Da LogP 1.49 TPSA 108.7	✓ Ro5	✓ Clean	`CC(=O)c1cc(C(=O)O)c(C(C)=O)cc1C(=O)O`
ZINC8774595	0.706	472.6 Da LogP 3.54 TPSA 101.5	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)CSc1ncnc2ccc…`
ZINC9545965	0.706	456.5 Da LogP 2.22 TPSA 110.6	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)Cn1cnc2ccccc…`
ZINC95938319	0.706	252.2 Da LogP 0.85 TPSA 162.8	1 viol.	✓ Clean	`N=C(O)c1cc(C(=N)O)c(C(=O)O)cc1C(=O)O`
ZINC9951136	0.706	486.6 Da LogP 3.93 TPSA 101.5	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCCC2)cc1NC(=O)CSc1ncnc2cc…`
ZINC9715898	0.704	498.6 Da LogP 2.13 TPSA 138.5	✓ Ro5	✓ Clean	`Cc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)COC(=O)Cc1n[n…`
ZINC3456615	0.703	440.5 Da LogP 2.67 TPSA 112.2	✓ Ro5	✓ Clean	`O=C(Cc1n[nH]c(=O)c2ccccc12)Nc1ccc(S(=O)(=O)N2CC…`
ZINC1532902	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC15982245	0.700	366.4 Da LogP 2.07 TPSA 113.2	✓ Ro5	✓ Clean	`COc1ccc(NC(C)=O)cc1NC(=O)Cc1n[nH]c(=O)c2ccccc12`
ZINC2018106	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC13141133	0.698	464.6 Da LogP 4.72 TPSA 75.7	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)Cc1ccc(-c2cc…`
ZINC5558991	0.698	406.5 Da LogP 3.19 TPSA 75.7	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCC2)cc1NC(=O)Cc1ccccc1F`
ZINC6712092	0.698	387.5 Da LogP 2.61 TPSA 91.5	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N(C)C)cc1NC(=O)Cc1c[nH]c2ccccc…`
ZINC6871244	0.698	420.5 Da LogP 3.58 TPSA 75.7	✓ Ro5	✓ Clean	`COc1ccc(S(=O)(=O)N2CCCCCC2)cc1NC(=O)Cc1ccccc1F`
ZINC13112605	0.697	440.5 Da LogP 2.67 TPSA 112.2	✓ Ro5	✓ Clean	`O=C(Cc1n[nH]c(=O)c2ccccc12)Nc1cccc(S(=O)(=O)N2C…`

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.