Protein profile

PA1581

succinate dehydrogenase subunit C

Genome: NC_002516.2

Gene: sdhC PA1581 Structure source: AlphaFold UniProt Q9I3D7
Amino acids 128
Annotations 8
Features 28
PDB binders 32
Druggability 0.854

Overview

Basic information about this protein and its source genome.

Accession
PA1581
Gene
sdhC PA1581
Status
annotated
Amino acids
128
Structure source
AlphaFold

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
31.373
Human E-value
7.58e-06
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
CytoplasmicMembrane

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 0.854
Structure
Pocket

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Gene Ontology (GO)

8
  • GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
  • GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways.
  • GO:0046872 Binding to a metal ion.
  • 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:0000104 Catalysis of the reaction: succinate + acceptor = fumarate + reduced acceptor.
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
  • GO:0045281 OBSOLETE. A multimeric complex which consists of flavoprotein (subunit A ; InterPro:IPR003952), iron-sulfur protein (subunit B) and membrane-bound cytochrome b560 (subunit C; InterPro:IPR000701). In some Archaea, the membrane-bound subunits (C or C and D) do not necessarily contain heme. Membrane-bound subunits can bind or react with quinones.

Sequence Features

Domain/signature hits from InterPro and related databases.

28 records
Show feature table
Start End DB Term Name
72 94 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
107 126 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
108 127 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
3 123 PANTHER PTHR10978 SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT
3 123 InterPro IPR014314 Succinate dehydrogenase, cytochrome b556 subunit
88 107 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
9 33 ProSitePatterns PS01000 Succinate dehydrogenase cytochrome b subunit signature 1.
9 33 InterPro IPR018495 Succinate dehydrogenase, cytochrome b subunit, conserved site
28 48 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
1 128 SUPERFAMILY SSF81343 Fumarate reductase respiratory complex transmembrane subunits
1 128 InterPro IPR034804 Fumarate reductase/succinate dehydrogenase, transmembrane subunit
1 128 Gene3D G3DSA:1.20.1300.10 Fumarate reductase/succinate dehydrogenase, transmembrane subunit
26 48 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
1 128 PIRSF PIRSF000178 SDH_cyt_b560
1 128 InterPro IPR014314 Succinate dehydrogenase, cytochrome b556 subunit
1 27 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
84 97 ProSitePatterns PS01001 Succinate dehydrogenase cytochrome b subunit signature 2.
84 97 InterPro IPR018495 Succinate dehydrogenase, cytochrome b subunit, conserved site
49 67 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1 128 FunFam G3DSA:1.20.1300.10:FF:000005 Succinate dehydrogenase cytochrome b556 subunit
8 126 NCBIfam TIGR02970 succinate dehydrogenase, cytochrome b556 subunit
8 126 InterPro IPR014314 Succinate dehydrogenase, cytochrome b556 subunit
9 125 CDD cd03499 SQR_TypeC_SdhC
9 125 InterPro IPR014314 Succinate dehydrogenase, cytochrome b556 subunit
6 122 Pfam PF01127 Succinate dehydrogenase/Fumarate reductase transmembrane subunit
6 122 InterPro IPR000701 Succinate dehydrogenase/fumarate reductase type B, transmembrane subunit
68 87 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
128 128 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

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

0 + 1

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA1581
AlphaFold 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
2 0.854
4 0.843
3 0.222

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.

82 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
11J D0VWV4 399.2 Da LogP 5.21 TPSA 29.1 1 viol. ✓ Clean c1ccc(cc1)c2cccc(c2)NC(=O)c3ccccc3I
12J D0VWV4 381.2 Da LogP 4.33 TPSA 38.3 ✓ Ro5 ✓ Clean CC(C)Oc1cccc(c1)NC(=O)c2ccccc2I
3NP D0VWV4 119.1 Da LogP -0.26 TPSA 80.4 ✓ Ro5 ✓ Clean C(C[N+](=O)[O-])C(=O)O
AT5 P69054 366.2 Da LogP 2.79 TPSA 88.6 ✓ Ro5 ✓ Clean C[C@@H](C[C@H](C)C(=O)C1=C(C(=C(NC1=O)OC)OC)O)[…
BOL D0VWV4 323.1 Da LogP 3.54 TPSA 29.1 ✓ Ro5 ✓ Clean c1ccc(cc1)NC(=O)c2ccccc2I
CBE P69054 235.3 Da LogP 2.62 TPSA 38.3 ✓ Ro5 ✓ Clean CC1=C(SCCO1)C(=O)Nc2ccccc2
CDN P69054 1151.5 Da LogP 14.77 TPSA 249.6 4 viol. ✓ Clean CCCCCCCCCCCCCCC(O)O[C@H](COC(CCCCC)O)CO[P@@](=O…
DNT P69054 282.3 Da LogP 3.89 TPSA 106.5 ✓ Ro5 ✓ Clean CCCCCC(C)c1cc(cc(c1O)[N+](=O)[O-])[N+](=O)[O-]
E23 D0VWV4 335.4 Da LogP 4.93 TPSA 29.1 ✓ Ro5 ✓ Clean CC(C)(C)c1ccc(cc1)CNC(=O)c2ccccc2C(F)(F)F
EBM D0VWV4 289.1 Da LogP 2.43 TPSA 29.1 ✓ Ro5 ✓ Clean CC(C)NC(=O)c1ccccc1I
EPH P69054 709.9 Da LogP 10.16 TPSA 134.4 2 viol. ✓ Clean CCCC=CCC=CCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCC=CCC…
F3S P69054 295.8 Da LogP 2.59 TPSA 0.0 ✓ Ro5 ✓ Clean S1[Fe]2S[Fe]3[S]2[Fe]1S3
F6A D0VWV4 341.3 Da LogP 5.62 TPSA 29.1 1 viol. ✓ Clean c1ccc(cc1)c2cccc(c2)NC(=O)c3ccccc3C(F)(F)F
F7A D0VWV4 357.3 Da LogP 5.75 TPSA 38.3 1 viol. ✓ Clean c1ccc(cc1)Oc2cccc(c2)NC(=O)c3ccccc3C(F)(F)F
F9A D0VWV4 322.3 Da LogP 4.02 TPSA 32.3 ✓ Ro5 ✓ Clean CN(C)Cc1cccc(c1)NC(=O)c2ccccc2C(F)(F)F
FD8 D0VWV4 447.3 Da LogP 6.45 TPSA 38.3 1 viol. ✓ Clean c1ccc(c(c1)C(=O)Nc2cccc(c2)Oc3c(c(c(c(c3F)F)F)F…
FES P69054 175.8 Da LogP 1.29 TPSA 0.0 ✓ Ro5 ✓ Clean S1[Fe]S[Fe]1
FTN D0VWV4 323.3 Da LogP 4.74 TPSA 38.3 ✓ Ro5 ✓ Clean CC(C)Oc1cccc(c1)NC(=O)c2ccccc2C(F)(F)F
JMP D0VWV4 299.3 Da LogP 3.42 TPSA 75.6 ✓ Ro5 ✓ Clean CC(C)Oc1cccc(c1)NC(=O)c2ccccc2C(=O)O
MLI D0VWV4 102.0 Da LogP -3.12 TPSA 80.3 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(=O)[O-]
MRN D0VWV4 269.3 Da LogP 4.03 TPSA 38.3 ✓ Ro5 ✓ Clean Cc1ccccc1C(=O)Nc2cccc(c2)OC(C)C
N1M D0VWV4 261.1 Da LogP 1.65 TPSA 29.1 ✓ Ro5 ✓ Clean CNC(=O)c1ccccc1I
NBI D0VWV4 242.2 Da LogP 2.85 TPSA 72.2 ✓ Ro5 ✓ Clean c1ccc(cc1)NC(=O)c2ccccc2[N+](=O)[O-]
OAA P69054 131.1 Da LogP -2.22 TPSA 94.5 ✓ Ro5 ✓ Clean C(C(=O)C(=O)O)C(=O)[O-]
PCI D0VWV4 266.3 Da LogP 4.66 TPSA 20.2 ✓ Ro5 ✓ Clean c1(c(c(c(c(c1Cl)Cl)Cl)Cl)Cl)O
SLI D0VWV4 213.2 Da LogP 2.64 TPSA 49.3 ✓ Ro5 ✓ Clean c1ccc(cc1)NC(=O)c2ccccc2O
TEO P69054 132.1 Da LogP -3.14 TPSA 103.7 ✓ Ro5 ✓ Clean C(=C(\O)/[O-])\[C@H](C(=O)[O-])O
TFZ D0VWV4 265.2 Da LogP 3.96 TPSA 29.1 ✓ Ro5 ✓ Clean c1ccc(cc1)NC(=O)c2ccccc2C(F)(F)F
TMG D0VWV4 201.3 Da LogP 2.69 TPSA 41.6 ✓ Ro5 ✓ Clean c1ccc2c(c1)[nH]c(n2)c3cscn3
TTF D0VWV4 222.2 Da LogP 2.45 TPSA 34.1 ✓ Ro5 ✓ Clean c1cc(sc1)C(=O)CC(=O)C(F)(F)F
UQ1 D0VWV4 250.3 Da LogP 2.32 TPSA 52.6 ✓ Ro5 Alert CC1=C(C(=O)C(=C(C1=O)OC)OC)CC=C(C)C
UQ2 P69054 318.4 Da LogP 4.04 TPSA 52.6 ✓ Ro5 Alert CC1=C(C(=O)C(=C(C1=O)OC)OC)C\C=C(/C)\CCC=C(C)C

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.