Protein profile

PA2851

elongation factor P

Genome: NC_002516.2

Gene: PA2851 efp Structure source: Experimental + AlphaFold UniProt Q9HZZ2
Amino acids 188
Annotations 5
Features 35
PDB binders 1
Druggability 0.797

Overview

Basic information about this protein and its source genome.

Accession
PA2851
Gene
PA2851 efp
Status
annotated
Amino acids
188
Structure source
Experimental + AlphaFold

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
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 0.797
Structure
Pocket

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0003746 Functions in chain elongation during polypeptide synthesis at the ribosome.
  • GO:0043043 The chemical reactions and pathways resulting in the formation of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. This may include the translation of a precursor protein and its subsequent processing into a functional peptide.
  • GO:0006414 The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis.

Sequence Features

Domain/signature hits from InterPro and related databases.

35 records
Show feature table
Start End DB Term Name
130 186 SUPERFAMILY SSF50249 Nucleic acid-binding proteins
130 186 InterPro IPR012340 Nucleic acid-binding, OB-fold
130 185 Pfam PF09285 Elongation factor P, C-terminal
130 185 InterPro IPR015365 Elongation factor P, C-terminal
1 186 Hamap MF_00141 Elongation factor P [efp].
1 186 InterPro IPR011768 Translation elongation factor P
66 127 CDD cd04470 S1_EF-P_repeat_1
66 127 InterPro IPR001059 Translation elongation factor P/YeiP, central
130 185 SMART SM00841 Elong_fact_P_C_2
1 63 FunFam G3DSA:2.30.30.30:FF:000003 Elongation factor P
3 186 NCBIfam TIGR00038 elongation factor P
3 186 InterPro IPR011768 Translation elongation factor P
130 185 CDD cd05794 S1_EF-P_repeat_2
1 63 Gene3D G3DSA:2.30.30.30 -
1 63 InterPro IPR014722 Ribosomal protein L2, domain 2
129 188 Gene3D G3DSA:2.40.50.140 -
129 188 InterPro IPR012340 Nucleic acid-binding, OB-fold
64 128 FunFam G3DSA:2.40.50.140:FF:000009 Elongation factor P
1 187 PIRSF PIRSF005901 EF-P
1 187 InterPro IPR020599 Translation elongation factor P/YeiP
3 185 PANTHER PTHR30053 ELONGATION FACTOR P
3 185 InterPro IPR020599 Translation elongation factor P/YeiP
64 128 Gene3D G3DSA:2.40.50.140 -
64 128 InterPro IPR012340 Nucleic acid-binding, OB-fold
67 122 SMART SM01185 EFP_2
67 122 InterPro IPR001059 Translation elongation factor P/YeiP, central
3 60 Pfam PF08207 Elongation factor P (EF-P) KOW-like domain
3 60 InterPro IPR013185 Translation elongation factor, KOW-like
129 187 FunFam G3DSA:2.40.50.140:FF:000004 Elongation factor P
1 62 SUPERFAMILY SSF50104 Translation proteins SH3-like domain
1 62 InterPro IPR008991 Translation protein SH3-like domain superfamily
68 122 Pfam PF01132 Elongation factor P (EF-P) OB domain
68 122 InterPro IPR001059 Translation elongation factor P/YeiP, central
65 128 SUPERFAMILY SSF50249 Nucleic acid-binding proteins
65 128 InterPro IPR012340 Nucleic acid-binding, OB-fold

3D Structure

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

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Structural evidence

2 + 1

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

Entry Method Resolution Chain Coverage Links Status
PDB 3OYY
X-ray 1.75 Å A,B
100.0% 1-188
Viewing
PDB 6J7M
X-ray 2.30 Å M,N
100.0% 1-188
Loaded
AlphaFold PA2851
AlphaFold full sequence Loaded
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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
KAA P0A6N4 474.5 Da LogP -3.14 TPSA 243.8 2 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.