Protein profile

KP13_00201

ADP-heptose--LPS heptosyltransferase 2

Genome: KpKP13

Gene: AHE42115.1 rfaF Structure source: AlphaFold + ColabFold UniProt A0A0H3H038
Amino acids 342
Annotations 6
Features 12
PDB binders 1
Druggability 0.05

Overview

Basic information about this protein and its source genome.

Accession
KP13_00201
Gene
AHE42115.1 rfaF
Status
annotated
Amino acids
342
Structure source
AlphaFold + ColabFold

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
88.69
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
91.66

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 0.05
Structure A0A0H3H038
Pocket Pocket 25
P2Rank 0.861
Structure A0A0H3H038
Pocket Pocket 1
ColabFold model
FPocket 0.366 · Pocket 28
P2Rank 0.828 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 144 / 4744 genomes with a hit
Normalized 0.03

Sequence

Primary amino-acid sequence viewer.

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:0009103 The chemical reactions and pathways resulting in the formation of lipopolysaccharides, any of a group of related, structurally complex components of the outer membrane of Gram-negative bacteria.
  • GO:0016757 Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0008713 Catalysis of the reaction: heptosyl-KDO2-lipid A + ADP-L-glycero-beta-D-manno-heptose = heptosyl2-KDO2-lipid A + ADP + H+.
  • GO:0009244 The chemical reactions and pathways resulting in the formation of the core region of bacterial lipopolysaccharides, which contains ten saccharide residues.

Sequence Features

Domain/signature hits from InterPro and related databases.

12 records
Show feature table
Start End DB Term Name
153 337 Gene3D G3DSA:3.40.50.2000 Glycogen Phosphorylase B;
155 334 FunFam G3DSA:3.40.50.2000:FF:000023 ADP-heptose--LPS heptosyltransferase II
59 314 Pfam PF01075 Glycosyltransferase family 9 (heptosyltransferase)
59 314 InterPro IPR002201 Glycosyl transferase, family 9
1 141 Gene3D G3DSA:3.40.50.2000 Glycogen Phosphorylase B;
1 140 FunFam G3DSA:3.40.50.2000:FF:000022 ADP-heptose--LPS heptosyltransferase II
1 337 PANTHER PTHR30160 TETRAACYLDISACCHARIDE 4'-KINASE-RELATED
1 335 SUPERFAMILY SSF53756 UDP-Glycosyltransferase/glycogen phosphorylase
1 333 NCBIfam TIGR02195 lipopolysaccharide heptosyltransferase II
1 333 InterPro IPR011910 ADP-heptose--LPS heptosyltransferase 2
1 331 CDD cd03789 GT9_LPS_heptosyltransferase
1 331 InterPro IPR002201 Glycosyl transferase, family 9

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 + 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_A0A0H3H038
AlphaFold full sequence Viewing
ColabFold KP13_00201
ColabFold full sequence Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

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 15.2 0.748
2 6.14 0.305
3 5.95 0.292
4 3.8 0.147
5 1.63 0.026

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.

51 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
AFH P24173 621.4 Da LogP -3.58 TPSA 311.7 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…

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.