Protein target profile

HT085_RS00200

glutamate-1-semialdehyde 2,1-aminomutase

Genome: NZ_AP023069.1 Gene: ESCNG_30012 TUM19854C_00330 hemL E8M63_03335 N776_09140 NGO_0040 3D evidence: AlphaFold DB model UniProt Q5FAH9 UniProt A0AA44ZGS4 UniProt A0AAQ1IMH4
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Length 426
Direct ligand evidence 0 56 total records
Functional annotation 1 EC 5 GO
Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Structure available AlphaFold DB model Ligand evidence via structure/bioactivity 6 structural and 0 bioactivity records.

Risks to review

Human similarity A significant human homolog was found.

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein. No FPocket pocket score No selected computational pocket-druggability value is available.
Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target
Hit
Gut microbiome off-target
Hit

Essentiality

Essential (DEG)
Y

Localization

Localization
Cytoplasmic

Binding-site evidence

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket Medium
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MNRNEILFDRAKAIIPGGVNSPVRAFGSVGGVPRFIKKAEGAYVWDENGTRYTDYVGSWGPAIVGHAHPEVVEAVREAALGGLSFGAPTEGEIAIAEQIAEIMPSVERLRLVSSGTEATMTAIRLARGFTGRDKIIKFEGCYHGHSDSLLVKAGSGLLTFGNPSSAGVPADFTKHTLVLEYNNIAQLEEAFAQSGDEIACVIVEPFVGNMNLVRPTEAFVKALRGLTEKHGAVLIYDEVMTGFRVALGGAQSLHGITPDLTTMGKVIGGGMPLAAFGGRKDIMECISPLGGVYQAGTLSGNPIAVAAGLKTLEIIQREGFYENLTALTQRLANGIAAAKAHGIEFAADSVGGMFGLYFAAHVPRNYADMARSNIDAFKRFFHGMLDRGIAFGPSAYEAGFVSAAHTPELIDETVAVAVEVFKAMAA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

5
  • GO:0008483 Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.
  • 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:0042286 Catalysis of the reaction: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0006782 The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

18 records
Show feature table
Start End DB Term Name
5 423 NCBIfam TIGR00713 glutamate-1-semialdehyde 2,1-aminomutase
5 423 InterPro IPR004639 Tetrapyrrole biosynthesis, glutamate-1-semialdehyde aminotransferase
7 421 CDD cd00610 OAT_like
7 421 InterPro IPR005814 Aminotransferase class-III
69 317 FunFam G3DSA:3.40.640.10:FF:000021 Glutamate-1-semialdehyde 2,1-aminomutase
2 423 PANTHER PTHR43713 GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE
32 394 Pfam PF00202 Aminotransferase class-III
32 394 InterPro IPR005814 Aminotransferase class-III
69 317 Gene3D G3DSA:3.40.640.10 -
69 317 InterPro IPR015421 Pyridoxal phosphate-dependent transferase, major domain
234 270 ProSitePatterns PS00600 Aminotransferases class-III pyridoxal-phosphate attachment site.
234 270 InterPro IPR005814 Aminotransferase class-III
2 423 SUPERFAMILY SSF53383 PLP-dependent transferases
2 423 InterPro IPR015424 Pyridoxal phosphate-dependent transferase
7 416 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
7 416 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small domain
3 424 Hamap MF_00375 Glutamate-1-semialdehyde 2,1-aminomutase [hemL].
3 424 InterPro IPR004639 Tetrapyrrole biosynthesis, glutamate-1-semialdehyde aminotransferase

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low
How colors and pocket overlays are used
Uniform protein color marks the displayed model as a single molecular object.
Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.
Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.
Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #2
0.566
Likely same site as P2Rank 2 2.4 Å 15 shared residues 100% of smaller site
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Surrounding area
Site 2 FPocket #1
0.369
Likely same site as P2Rank 1 2.1 Å 21 shared residues 95% of smaller site
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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1
0.662
Likely same site as FPocket 1 2.1 Å 21 shared residues 95% of smaller site
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Surrounding area
Site 2 P2Rank #2
0.649
Likely same site as FPocket 2 2.4 Å 15 shared residues 100% of smaller site
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Surrounding area
Site 3 P2Rank #3
0.27
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Surrounding area
Site 4 P2Rank #4
0.045
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Surrounding area
Site 5 P2Rank #5
0.035
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Surrounding area
All structural evidence 0 experimental · 1 predicted

Structural evidence

0 + 1

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold DB HT085_RS00200
AlphaFold DB — — full sequence — Viewing

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.

56 records
Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records
Transferred evidence 6 records from similar proteins
Structural ligands 6 0 loaded crystals
Measured bioactivity 0 direct and transferred ChEMBL records
Proposed compounds 50 similarity-based ZINC candidates
Best available ligand signal
EA5 PDB via homolog 363.3 Da · LogP -0.01 · TPSA 175.2 Open detail RCSB PDB
GAB PDB via homolog Detail RCSB PDB
HOZ PDB via homolog Detail RCSB PDB
KE4 PDB via homolog Detail RCSB PDB
PLR PDB via homolog Detail RCSB PDB

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
EA5 RCSB PDB
2HP1
P24630 363.3 Da LogP -0.01 TPSA 175.2 1 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CNC[C@H](CCC(=O)O)N)O
GAB RCSB PDB
3GSB
P24630 137.1 Da LogP 0.97 TPSA 63.3 ✓ Ro5 ✓ Clean c1cc(cc(c1)N)C(=O)O
HOZ RCSB PDB
2HOZ
P24630 132.2 Da LogP -0.86 TPSA 89.3 ✓ Ro5 ✓ Clean C(CC(=O)O)[C@@H](CN)N
KE4 RCSB PDB
2HP2
P24630 363.3 Da LogP -0.01 TPSA 175.2 1 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CNC(CCC(=O)O)CN)O
PLR RCSB PDB
3USF
Q31QJ2 233.2 Da LogP 1.01 TPSA 99.9 ✓ Ro5 ✓ Clean Cc1c(cnc(c1O)C)COP(=O)(O)O
PMP RCSB PDB
2GSA
P24630 248.2 Da LogP 0.16 TPSA 125.9 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN)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.