Protein profile

PA0761

L-aspartate oxidase

Genome: NC_002516.2

Gene: nadB PA0761 Structure source: AlphaFold UniProt Q51363
Export view
Amino acids 538
Annotations 7
Features 27
PDB binders 29
Druggability 0.255

Overview

Basic information about this protein and its source genome.

Accession
PA0761
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
nadB PA0761
Status
annotated
Amino acids
538
Structure source
AlphaFold
EC
1.4.3.16
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0008734 Catalysis of the reaction: L-aspartate + O2 = iminosuccinate + H2O2. Can also use fumatate as electron acceptor under anaerobic conditions, yielding succinate. GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. GO:0034628 The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD+), beginning with the catabolism of L-aspartate into the precursor quinolinate. NAD+ is a coenzyme that interconverts with its reduced form, NADH, in many redox and catabolic reactions. 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:0009435 The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD+), a coenzyme that interconverts with its reduced form, NADH, in many redox and catabolic reactions. NAD+ is derived from various sources including vitamin B3.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
34.038
Human E-value
1.0399999999999999e-60
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 0.255
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0008734 Catalysis of the reaction: L-aspartate + O2 = iminosuccinate + H2O2. Can also use fumatate as electron acceptor under anaerobic conditions, yielding succinate.
  • GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
  • GO:0034628 The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD+), beginning with the catabolism of L-aspartate into the precursor quinolinate. NAD+ is a coenzyme that interconverts with its reduced form, NADH, in many redox and catabolic reactions.
  • 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:0009435 The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD+), a coenzyme that interconverts with its reduced form, NADH, in many redox and catabolic reactions. NAD+ is derived from various sources including vitamin B3.

Sequence Features

Domain/signature hits from InterPro and related databases.

27 records
Show feature table
Start End DB Term Name
426 535 FunFam G3DSA:1.20.58.100:FF:000002 L-aspartate oxidase
248 361 Gene3D G3DSA:3.90.700.10 Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
248 361 InterPro IPR027477 Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
248 361 FunFam G3DSA:3.90.700.10:FF:000002 L-aspartate oxidase
238 353 SUPERFAMILY SSF56425 Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
238 353 InterPro IPR027477 Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily
8 392 Pfam PF00890 FAD binding domain
8 392 InterPro IPR003953 FAD-dependent oxidoreductase 2, FAD binding domain
425 536 Gene3D G3DSA:1.20.58.100 -
3 448 SUPERFAMILY SSF51905 FAD/NAD(P)-binding domain
3 448 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
425 529 SUPERFAMILY SSF46977 Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain
425 529 InterPro IPR037099 Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain superfamily
6 520 NCBIfam TIGR00551 L-aspartate oxidase
6 520 InterPro IPR005288 L-aspartate oxidase
338 533 PIRSF PIRSF000171 SDHA_APRA_LASPO
1 323 PIRSF PIRSF000171 SDHA_APRA_LASPO
8 403 Gene3D G3DSA:3.50.50.60 -
8 403 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
4 531 PANTHER PTHR42716 L-ASPARTATE OXIDASE
4 531 InterPro IPR005288 L-aspartate oxidase
441 521 Pfam PF02910 Fumarate reductase flavoprotein C-term
441 521 InterPro IPR015939 Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal
453 473 Coils Coil Coil
355 377 PRINTS PR00368 FAD-dependent pyridine nucleotide reductase signature
9 28 PRINTS PR00368 FAD-dependent pyridine nucleotide reductase signature
8 261 FunFam G3DSA:3.50.50.60:FF:000060 L-aspartate oxidase

3D Structure

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

3D visualization script Full viewer

Loading 3D structure...

Legend High Medium Low

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 PA0761
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 0.255

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.

79 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
12J
4YSZ
Q33862 381.2 Da LogP 4.33 TPSA 38.3 ✓ Ro5 ✓ Clean CC(C)Oc1cccc(c1)NC(=O)c2ccccc2I
3NP
3P4S
P00363 119.1 Da LogP -0.26 TPSA 80.4 ✓ Ro5 ✓ Clean C(C[N+](=O)[O-])C(=O)O
3PE
6MYO
Q9YHT1 748.1 Da LogP 12.06 TPSA 134.4 2 viol. ✓ Clean CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN)OC…
4YP
5C2T
Q33862 303.4 Da LogP 3.35 TPSA 69.4 ✓ Ro5 Alert CC1=C(C(=O)C(=C(C1=O)N)OC)C/C=C(\C)/CCC=C(C)C
AT5
6MYS
Q9YHT1 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)[…
BRS
1KFY
P00363 322.7 Da LogP 4.01 TPSA 106.5 ✓ Ro5 ✓ Clean C[C@H](c1ccc(cc1)Cl)c2cc(cc(c2O)[N+](=O)[O-])[N…
CE1
1KF6
P00363 538.8 Da LogP 4.03 TPSA 94.1 1 viol. ✓ Clean CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCOCCO
E23
4YSX
Q33862 335.4 Da LogP 4.93 TPSA 29.1 ✓ Ro5 ✓ Clean CC(C)(C)c1ccc(cc1)CNC(=O)c2ccccc2C(F)(F)F
E24
4YSY
Q33862 348.2 Da LogP 4.94 TPSA 29.1 ✓ Ro5 ✓ Clean c1ccc(c(c1)C(=O)NCc2ccc(cc2Cl)Cl)C(F)(F)F
EPH
3VRA
Q33862 709.9 Da LogP 10.16 TPSA 134.4 2 viol. ✓ Clean CCCC=CCC=CCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCC=CCC…
F3S
3VRA
Q33862 295.8 Da LogP 2.59 TPSA 0.0 ✓ Ro5 ✓ Clean S1[Fe]2S[Fe]3[S]2[Fe]1S3
F6A
4YTM
Q33862 341.3 Da LogP 5.62 TPSA 29.1 1 viol. ✓ Clean c1ccc(cc1)c2cccc(c2)NC(=O)c3ccccc3C(F)(F)F
FD8
4YTN
Q33862 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
3VRA
Q33862 175.8 Da LogP 1.29 TPSA 0.0 ✓ Ro5 ✓ Clean S1[Fe]S[Fe]1
FLC
2B76
P00363 189.1 Da LogP -5.25 TPSA 140.6 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
FTN
3VRB
Q33862 323.3 Da LogP 4.74 TPSA 38.3 ✓ Ro5 ✓ Clean CC(C)Oc1cccc(c1)NC(=O)c2ccccc2C(F)(F)F
FUM
3VRB
Q33862 116.1 Da LogP -0.29 TPSA 74.6 ✓ Ro5 ✓ Clean C(=C/C(=O)O)\C(=O)O
GUA
3P4R
P00363 132.1 Da LogP 0.33 TPSA 74.6 ✓ Ro5 ✓ Clean C(CC(=O)O)CC(=O)O
HQO
1KF6
P00363 259.3 Da LogP 3.69 TPSA 47.2 ✓ Ro5 Alert CCCCCCCc1cc(c2ccccc2[n+]1[O-])O
MLI
3VRA
Q33862 102.0 Da LogP -3.12 TPSA 80.3 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(=O)[O-]
MQ7
1L0V
P00363 649.0 Da LogP 14.10 TPSA 34.1 2 viol. Alert CC1=C(C(=O)c2ccccc2C1=O)C\C=C(/C)\CC\C=C(/C)\CC…
MRN
4YT0
Q33862 269.3 Da LogP 4.03 TPSA 38.3 ✓ Ro5 ✓ Clean Cc1ccccc1C(=O)Nc2cccc(c2)OC(C)C
OAA
6MYO
Q9YHT1 131.1 Da LogP -2.22 TPSA 94.5 ✓ Ro5 ✓ Clean C(C(=O)C(=O)O)C(=O)[O-]
PBF
6B58
P00363 269.3 Da LogP 1.87 TPSA 80.4 ✓ Ro5 ✓ Clean c1ccc(cc1)C(=O)c2ccc(cc2)C[C@@H](C(=O)O)N
RQX
3VR8
Q33862 263.3 Da LogP 2.41 TPSA 69.4 ✓ Ro5 Alert CCC/C(=C/CC1=C(C(=O)C(=C(C1=O)OC)N)C)/C
SIN
1KNP
P10902 118.1 Da LogP -0.06 TPSA 74.6 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=O)O
TTF
6MYP
Q9YHT1 222.2 Da LogP 2.45 TPSA 34.1 ✓ Ro5 ✓ Clean c1cc(sc1)C(=O)CC(=O)C(F)(F)F
UMQ
6MYO
Q9YHT1 496.6 Da LogP -0.84 TPSA 178.5 2 viol. ✓ Clean CCCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1)…
UQ1
5C3J
Q33862 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

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.