Protein profile

PA1416

hypothetical protein

Genome: NC_002516.2

Gene: PA1416 Structure source: AlphaFold UniProt Q9I3S8
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Amino acids 460
Annotations 5
Features 19
PDB binders 13
Druggability 0.575

Overview

Basic information about this protein and its source genome.

Accession
PA1416
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1416
Status
annotated
Amino acids
460
Structure source
AlphaFold
GO
GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. GO:0022904 A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient. 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:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
47.619
Human E-value
1.12e-27
Gut microbiome off-target
hit
Essential (DEG)
N
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 0.575
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5
  • GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
  • GO:0022904 A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
  • 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:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.

Sequence Features

Domain/signature hits from InterPro and related databases.

19 records
Show feature table
Start End DB Term Name
338 418 Gene3D G3DSA:3.30.70.2740 -
220 334 Gene3D G3DSA:3.30.70.2190 -
190 459 SUPERFAMILY SSF55103 FAD-linked oxidases, C-terminal domain
190 459 InterPro IPR016164 FAD-linked oxidase-like, C-terminal
32 214 ProSiteProfiles PS51387 PCMH-type FAD-binding domain profile.
32 214 InterPro IPR016166 FAD-binding domain, PCMH-type
419 459 FunFam G3DSA:1.10.45.10:FF:000001 D-lactate dehydrogenase mitochondrial
419 459 Gene3D G3DSA:1.10.45.10 -
419 459 InterPro IPR016171 Vanillyl-alcohol oxidase, C-terminal subdomain 2
338 418 FunFam G3DSA:3.30.70.2740:FF:000010 FAD-binding oxidoreductase
42 175 Pfam PF01565 FAD binding domain
42 175 InterPro IPR006094 FAD linked oxidase, N-terminal
20 219 Gene3D G3DSA:3.30.465.10 -
20 219 InterPro IPR016169 FAD-binding, type PCMH, subdomain 2
7 460 PANTHER PTHR43716 D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL
218 458 Pfam PF02913 FAD linked oxidases, C-terminal domain
218 458 InterPro IPR004113 FAD-binding oxidoreductase/transferase, type 4, C-terminal
5 213 SUPERFAMILY SSF56176 FAD-binding/transporter-associated domain-like
5 213 InterPro IPR036318 FAD-binding, type PCMH-like superfamily

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 PA1416
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 0.575
1 0.279

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.

67 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
0SK
4F4Q
A0R607 417.4 Da LogP 3.21 TPSA 83.9 ✓ Ro5 ✓ Clean C[C@H]1COC2(O1)CCN(CC2)C3=NC(=O)c4cc(cc(c4S3)NO…
1DO
4BC7
P97275 186.3 Da LogP 3.90 TPSA 20.2 ✓ Ro5 ✓ Clean CCCCCCCCCCCCO
2HG
6LPP
Q8N465 148.1 Da LogP -0.70 TPSA 94.8 ✓ Ro5 ✓ Clean C(CC(=O)O)[C@H](C(=O)O)O
AKG
6LPX
Q8N465 146.1 Da LogP -0.50 TPSA 91.7 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=O)C(=O)O
AWB
5AE3
P97275 548.6 Da LogP 3.48 TPSA 157.3 1 viol. ✓ Clean CCCCCC[C@@H]1[C@H]([C@@H](OC(=O)[C@H]([C@H](OC1…
B2Z
5AE1
P97275 341.4 Da LogP 3.37 TPSA 77.8 ✓ Ro5 ✓ Clean C[C@@H](CC(=O)N[C@H](C)c1ccc2c(c1)NC(=O)N2)c3cc…
F6T
6GOU
P97275 345.3 Da LogP 2.94 TPSA 77.8 ✓ Ro5 ✓ Clean C[C@@H](CC(=O)NCc1ccc2c(c1)NC(=O)N2)c3c(cccc3F)F
FYC
5AE2
P97275 325.3 Da LogP 2.71 TPSA 77.8 ✓ Ro5 ✓ Clean C/C(=C\c1ccccc1F)/C(=O)NCc2ccc3c(c2)NC(=O)N3
KQS
5ADZ
P97275 327.4 Da LogP 2.81 TPSA 77.8 ✓ Ro5 ✓ Clean C[C@@H](CC(=O)NCc1ccc2c(c1)NC(=O)N2)c3ccccc3F
LAC
6LPT
Q8N465 90.1 Da LogP -0.55 TPSA 57.5 ✓ Ro5 ✓ Clean C[C@H](C(=O)O)O
MLT
6LPQ
Q8N465 134.1 Da LogP -1.09 TPSA 94.8 ✓ Ro5 ✓ Clean C([C@H](C(=O)O)O)C(=O)O
PL3
2UUU
O96759 242.4 Da LogP 5.46 TPSA 20.2 1 viol. ✓ Clean CCCCCCCCCCCCCCCCO
S2G
6LPU
Q8N465 148.1 Da LogP -0.70 TPSA 94.8 ✓ Ro5 ✓ Clean C(CC(=O)O)[C@@H](C(=O)O)O

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.