Protein profile

KP13_04181

Aspartate aminotransferase

Genome: KpKP13

Gene: aspC AHE45412.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GV21
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Amino acids 396
Annotations 11
Features 23
PDB binders 39
Druggability 0.431

Overview

Basic information about this protein and its source genome.

Accession
KP13_04181
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
aspC AHE45412.1
Status
annotated
Amino acids
396
Structure source
AlphaFold + ColabFold
EC
2.6.1.-
GO
GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. GO:0008483 Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid. GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups. GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones. 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:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
42.748
Human E-value
6.22e-101
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
63.131
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
96.61

Selected Druggability evidence

AlphaFold / UniProt model

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 0.431
Structure A0A0H3GV21
Pocket Pocket 6
P2Rank 0.913
Structure A0A0H3GV21
Pocket Pocket 1
ColabFold model
FPocket 0.412 · Pocket 5
P2Rank 0.87 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 174 / 4744 genomes with a hit
Normalized 0.037

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

10
  • GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
  • GO:0008483 Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.
  • GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
  • GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
  • 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:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0042802 Binding to an identical protein or proteins.
  • GO:0004069 Catalysis of the reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
  • GO:0004838 Catalysis of the reaction: L-tyrosine + 2-oxoglutarate = 3-(4-hydroxyphenyl)pyruvate + L-glutamate.
  • GO:0033585 OBSOLETE. The chemical reactions and pathways resulting in the formation of L-phenylalanine from other compounds, including chorismate, via the intermediate phenylpyruvate.

Sequence Features

Domain/signature hits from InterPro and related databases.

23 records
Show feature table
Start End DB Term Name
27 392 Pfam PF00155 Aminotransferase class I and II
27 392 InterPro IPR004839 Aminotransferase, class I/classII
243 256 ProSitePatterns PS00105 Aminotransferases class-I pyridoxal-phosphate attachment site.
243 256 InterPro IPR004838 Aminotransferases, class-I, pyridoxal-phosphate-binding site
175 194 PRINTS PR00799 Aspartate aminotransferase signature
175 194 InterPro IPR000796 Aspartate/other aminotransferase
341 359 PRINTS PR00799 Aspartate aminotransferase signature
341 359 InterPro IPR000796 Aspartate/other aminotransferase
273 298 PRINTS PR00799 Aspartate aminotransferase signature
273 298 InterPro IPR000796 Aspartate/other aminotransferase
206 218 PRINTS PR00799 Aspartate aminotransferase signature
206 218 InterPro IPR000796 Aspartate/other aminotransferase
1 396 SUPERFAMILY SSF53383 PLP-dependent transferases
1 396 InterPro IPR015424 Pyridoxal phosphate-dependent transferase
5 392 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
5 392 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small domain
60 300 FunFam G3DSA:3.40.640.10:FF:000015 Aspartate aminotransferase
60 300 Gene3D G3DSA:3.40.640.10 -
60 300 InterPro IPR015421 Pyridoxal phosphate-dependent transferase, major domain
29 392 CDD cd00609 AAT_like
1 395 PANTHER PTHR11879 ASPARTATE AMINOTRANSFERASE
1 395 InterPro IPR000796 Aspartate/other aminotransferase
289 392 FunFam G3DSA:3.90.1150.10:FF:000001 Aspartate aminotransferase

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

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Structural evidence

0 + 2

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GV21
AlphaFold — — full sequence — Viewing
ColabFold KP13_04181
ColabFold — — full sequence — Loaded
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
6 0.431

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 20.7 0.86
2 2.85 0.089
3 1.36 0.016
4 0.78 0.002

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.

90 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
0A0
1ART
P00509 147.1 Da LogP -0.74 TPSA 100.6 ✓ Ro5 ✓ Clean C[C@](CC(=O)O)(C(=O)O)N
3IB
2AY6
P95468 203.2 Da LogP 2.58 TPSA 53.1 ✓ Ro5 ✓ Clean c1ccc2c(c1)c(c[nH]2)CCCC(=O)O
3QP
3QPG
P00509 361.2 Da LogP 0.66 TPSA 173.9 ✓ Ro5 ✓ Clean Cc1ccc(c(c1O)/C=N/[C@@H](CC(=O)O)C(=O)O)COP(=O)…
4TB
2AY8
P95468 170.2 Da LogP 2.16 TPSA 37.3 ✓ Ro5 ✓ Clean c1cc(sc1)CCCC(=O)O
5PV
2AY9
P95468 178.2 Da LogP 2.48 TPSA 37.3 ✓ Ro5 ✓ Clean c1ccc(cc1)CCCCC(=O)O
77E
5T4L
P00509 348.3 Da LogP 0.83 TPSA 163.2 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CC[C@H](CCC(=O)O)N)O
AHC
2AY1
P95468 165.2 Da LogP 1.29 TPSA 63.3 ✓ Ro5 Alert c1cc(ccc1CCC(=O)O)N
AKG
1AIB
P00509 146.1 Da LogP -0.50 TPSA 91.7 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=O)C(=O)O
CLT
2AY7
P95468 164.2 Da LogP 2.09 TPSA 37.3 ✓ Ro5 ✓ Clean c1ccc(cc1)CCCC(=O)O
CXP
2AY2
P95468 156.2 Da LogP 2.43 TPSA 37.3 ✓ Ro5 ✓ Clean C1CCC(CC1)CCC(=O)O
GUA
1AMS
P00509 132.1 Da LogP 0.33 TPSA 74.6 ✓ Ro5 ✓ Clean C(CC(=O)O)CC(=O)O
HCI
1AHX
P00509 150.2 Da LogP 1.70 TPSA 37.3 ✓ Ro5 ✓ Clean c1ccc(cc1)CCC(=O)O
IOP
1AHF
P00509 189.2 Da LogP 2.19 TPSA 53.1 ✓ Ro5 ✓ Clean c1ccc2c(c1)c(c[nH]2)CCC(=O)O
IVA
1YOO
P00509 102.1 Da LogP 1.12 TPSA 37.3 ✓ Ro5 ✓ Clean CC(C)CC(=O)O
KET
4RKD
C7E5X4 363.2 Da LogP -0.53 TPSA 188.1 ✓ Ro5 ✓ Clean Cc1c(c(c(c[nH+]1)COP(=O)(O)O)C=NC(CC(=O)O)C(=O)…
KYN
3PD6
P05202 208.2 Da LogP 0.25 TPSA 106.4 ✓ Ro5 ✓ Clean c1ccc(c(c1)C(=O)C[C@@H](C(=O)O)N)N
LMR
6T3V
C7E5X4 134.1 Da LogP -1.09 TPSA 94.8 ✓ Ro5 ✓ Clean C([C@@H](C(=O)O)O)C(=O)O
MAE
1AHY
P00509 116.1 Da LogP -0.29 TPSA 74.6 ✓ Ro5 ✓ Clean C(=C/C(=O)O)/C(=O)O
MPL
1ASD
P00509 262.2 Da LogP -0.05 TPSA 107.9 ✓ Ro5 ✓ Clean Cc1c(c(c(c[n+]1C)COP(=O)(O)O)C=O)O
MPP
2AY3
P95468 210.2 Da LogP 1.72 TPSA 55.8 ✓ Ro5 ✓ Clean COc1ccc(cc1OC)CCC(=O)O
NOP
1ASE
P00509 263.1 Da LogP -0.24 TPSA 131.0 ✓ Ro5 ✓ Clean Cc1c(c(c(c[n+]1[O-])COP(=O)(O)O)C=O)O
NPL
1ASC
P00509 263.2 Da LogP -0.41 TPSA 116.9 ✓ Ro5 ✓ Clean Cc1c(c(c(c[n+]1C)COP(=O)(O)O)CN)O
OAA
3PDB
P05202 131.1 Da LogP -2.22 TPSA 94.5 ✓ Ro5 ✓ Clean C(C(=O)C(=O)O)C(=O)[O-]
PDG
1X2A
P00509 378.3 Da LogP 0.11 TPSA 186.5 1 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@H](CCC(=O)O)C(=O)…
PGU
1X28
P00509 378.3 Da LogP 0.11 TPSA 186.5 1 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CCC(=O)O)C(=O…
PJ7
3PA9
D3H0F7 127.1 Da LogP 0.56 TPSA 76.5 ✓ Ro5 ✓ Clean c1c(coc1C(=O)O)N
PL6
5VWR
P00509 376.3 Da LogP 0.44 TPSA 186.8 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)\C=N\[C@@H](CCC(=O)O)C…
PLA
1ASL
P00509 378.3 Da LogP 0.11 TPSA 186.5 1 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@](C)(CC(=O)O)C(=…
PLR
3FSL
P04693 233.2 Da LogP 1.01 TPSA 99.9 ✓ Ro5 ✓ Clean Cc1c(cnc(c1O)C)COP(=O)(O)O
PMG
1X29
P00509 392.3 Da LogP 0.50 TPSA 186.5 1 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@](C)(CCC(=O)O)C(…
PMP
1AIA
P00509 248.2 Da LogP 0.16 TPSA 125.9 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN)O
PP3
1C9C
P00509 320.2 Da LogP 0.27 TPSA 149.2 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](C)C(=O)O)O
PPD
1ARG
P00509 364.2 Da LogP -0.28 TPSA 186.5 1 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CC(=O)O)C(=O)…
PPT
2AY4
P95468 164.2 Da LogP 2.01 TPSA 37.3 ✓ Ro5 ✓ Clean Cc1ccc(cc1)CCC(=O)O
PSZ
2QBT
P00509 374.3 Da LogP 2.08 TPSA 149.2 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CNc2cc(sc2)C(=O)O)O
PY4
1CQ6
P00509 334.3 Da LogP 0.66 TPSA 149.2 ✓ Ro5 ✓ Clean CC[C@H](C(=O)O)NCc1c(cnc(c1O)C)COP(=O)(O)O
PY5
1CQ7
P00509 348.3 Da LogP 1.05 TPSA 149.2 ✓ Ro5 ✓ Clean CCC[C@@H](C(=O)O)NCc1c(cnc(c1O)C)COP(=O)(O)O
PY6
1CQ8
P00509 362.3 Da LogP 1.44 TPSA 149.2 ✓ Ro5 ✓ Clean CCCC[C@@H](C(=O)O)NCc1c(cnc(c1O)C)COP(=O)(O)O
SIN
1CZE
P00509 118.1 Da LogP -0.06 TPSA 74.6 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=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.