Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: KP13_02457
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE43107.1
Status: annotated
Amino acids: 222
Structure source: AlphaFold + ColabFold

GO

GO:0061077 OBSOLETE. The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone. GO:0043711 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a pilus, a short filamentous structure on a bacterial cell, flagella-like in structure and generally present in many copies. GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall. GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Periplasmic
ColabFold pLDDT: 91.95

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 0.218

Structure A0A377Z6I2

Pocket Pocket 4

P2Rank

Structure A0A377Z6I2

Pocket No pockets

ColabFold model

FPocket 0.162 · Pocket 10

P2Rank 0.005 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 4 / 4744 genomes with a hit

Normalized 0.001

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

4

GO:0061077 OBSOLETE. The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
GO:0043711 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a pilus, a short filamentous structure on a bacterial cell, flagella-like in structure and generally present in many copies.
GO:0030288 The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.
GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.

Sequence Features

Domain/signature hits from InterPro and related databases.

31 records

Show feature table

Start	End	DB	Term	Name
117	132	PRINTS	PR00969	Pili chaperone signature
117	132	InterPro	IPR001829	Pili assembly chaperone, bacterial
20	29	PRINTS	PR00969	Pili chaperone signature
20	29	InterPro	IPR001829	Pili assembly chaperone, bacterial
152	167	PRINTS	PR00969	Pili chaperone signature
152	167	InterPro	IPR001829	Pili assembly chaperone, bacterial
66	87	PRINTS	PR00969	Pili chaperone signature
66	87	InterPro	IPR001829	Pili assembly chaperone, bacterial
94	111	PRINTS	PR00969	Pili chaperone signature
94	111	InterPro	IPR001829	Pili assembly chaperone, bacterial
20	135	Pfam	PF00345	Pili and flagellar-assembly chaperone, PapD N-terminal domain
20	135	InterPro	IPR016147	Pili assembly chaperone, N-terminal
15	18	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
1	2	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
1	18	Phobius	SIGNAL_PEPTIDE	Signal peptide region
1	18	SignalP_EUK	SignalP-noTM	SignalP-noTM
139	218	SUPERFAMILY	SSF49584	Periplasmic chaperone C-domain
139	218	InterPro	IPR036316	Pili assembly chaperone, C-terminal domain superfamily
93	110	ProSitePatterns	PS00635	Gram-negative pili assembly chaperone signature.
93	110	InterPro	IPR018046	Pili assembly chaperone, conserved site
19	135	Gene3D	G3DSA:2.60.40.10	Immunoglobulins
19	135	InterPro	IPR013783	Immunoglobulin-like fold
16	135	SUPERFAMILY	SSF49354	PapD-like
16	135	InterPro	IPR008962	PapD-like superfamily
3	216	PANTHER	PTHR30251	PILUS ASSEMBLY CHAPERONE
3	14	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
158	216	Pfam	PF02753	Pili assembly chaperone PapD, C-terminal domain
158	216	InterPro	IPR016148	Pili assembly chaperone, C-terminal
139	221	Gene3D	G3DSA:2.60.40.10	Immunoglobulins
139	221	InterPro	IPR013783	Immunoglobulin-like fold
19	222	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.

3D Structure

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

Loading 3D structure...

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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_A0A377Z6I2	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_02457	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
4				0.218

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.

3 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

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.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
EC2	2XG5	P15319	453.6 Da LogP 5.94 TPSA 59.3	1 viol.	✓ Clean	`c1ccc(cc1)[C@@H]2[C@H](N3C(=O)C=C(C(=C3S2)C4CC4…`
EC5	2XG5	P15319	471.6 Da LogP 5.90 TPSA 79.5	1 viol.	✓ Clean	`c1ccc(cc1)C[C@@H](C(=O)O)N2C(=O)C=C(C(=C2SO)C3C…`
XC2	2XG4	P15319	476.6 Da LogP 4.03 TPSA 71.8	✓ Ro5	✓ Clean	`c1ccc2c(c1)cccc2CC3=C(C(=O)N4[C@@H](CSC4=C3C5CC…`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

No virtual-screening candidates for this protein.

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.

KP13_02457