Protein profile

KP13_04629

Cysteine desulfurase bifunctional protein

Genome: KpKP13

Gene: AHE44111.1 sufS Structure source: AlphaFold + ColabFold UniProt A0A0H3GPH5
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Amino acids 406
Annotations 4
Features 18
PDB binders 9
Druggability 0.513

Overview

Basic information about this protein and its source genome.

Accession
KP13_04629
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE44111.1 sufS
Status
annotated
Amino acids
406
Structure source
AlphaFold + ColabFold
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:0031071 Catalysis of the reaction: L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine. GO:0006534 OBSOLETE. The chemical reactions and pathways involving cysteine, 2-amino-3-mercaptopropanoic acid. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
32.075
Human E-value
5.47e-07
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
51.613
DEG E-value
1.22e-149
Localization
Cytoplasmic
ColabFold pLDDT
98.02

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 0.513
Structure A0A0H3GPH5
Pocket Pocket 1
P2Rank 0.782
Structure A0A0H3GPH5
Pocket Pocket 1
ColabFold model
FPocket 0.284 · Pocket 1
P2Rank 0.783 · Pocket 1
Core conservation Accessory gene
Roary accessory
CoreCruncher accessory
Gut microbiome 383 / 4744 genomes with a hit
Normalized 0.081

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:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
  • GO:0031071 Catalysis of the reaction: L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine.
  • GO:0006534 OBSOLETE. The chemical reactions and pathways involving cysteine, 2-amino-3-mercaptopropanoic acid.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

18 records
Show feature table
Start End DB Term Name
25 398 CDD cd06453 SufS_like
25 398 InterPro IPR010970 Cysteine desulfurase, SufS
43 302 FunFam G3DSA:3.40.640.10:FF:000042 Cysteine desulfurase
7 405 NCBIfam TIGR01979 SufS family cysteine desulfurase
7 405 InterPro IPR010970 Cysteine desulfurase, SufS
25 394 Pfam PF00266 Aminotransferase class-V
25 394 InterPro IPR000192 Aminotransferase class V domain
10 396 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
10 396 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small domain
217 236 ProSitePatterns PS00595 Aminotransferases class-V pyridoxal-phosphate attachment site.
217 236 InterPro IPR020578 Aminotransferase class-V, pyridoxal-phosphate binding site
4 403 SUPERFAMILY SSF53383 PLP-dependent transferases
4 403 InterPro IPR015424 Pyridoxal phosphate-dependent transferase
5 402 PANTHER PTHR43586 CYSTEINE DESULFURASE
43 302 Gene3D G3DSA:3.40.640.10 -
43 302 InterPro IPR015421 Pyridoxal phosphate-dependent transferase, major domain
1 406 Hamap MF_01831 Cysteine desulfurase [sufS].
1 406 InterPro IPR010970 Cysteine desulfurase, SufS

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_A0A0H3GPH5
AlphaFold — — full sequence — Viewing
ColabFold KP13_04629
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
1 0.513
5 0.017
4 0.015
8 0.0

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 19.77 0.782
2 2.03 0.037
3 1.5 0.018
4 1.1 0.007

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.

59 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
7TS
7CES
O32164 331.2 Da LogP 0.60 TPSA 157.9 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CNC2=CONC2=O)O
C6P
5ZSO
O32164 352.3 Da LogP 0.18 TPSA 149.2 1 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CS)C(=O)O)O
CKT
6O13
P77444 350.3 Da LogP 0.66 TPSA 149.5 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)C/N=C(\CS)/C(=O)O)O
DCS
7CER
O32164 333.2 Da LogP -0.78 TPSA 150.2 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H]2CONC2=O)O
LPG
1I29
P77444 99.1 Da LogP -0.97 TPSA 63.3 ✓ Ro5 ✓ Clean C#CC(C(=O)O)N
PDA
5XT6
O32164 320.2 Da LogP 0.27 TPSA 149.2 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CNC(C)C(=O)O)O
PMP
7CEO
O32164 248.2 Da LogP 0.16 TPSA 125.9 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN)O
SEC
1KMK
P77444 168.1 Da LogP -1.28 TPSA 63.3 ✓ Ro5 ✓ Clean C([C@@H](C(=O)O)N)[SeH]
TLA
5FT5
Q46925 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@@H]([C@H](C(=O)O)O)(C(=O)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.