Overview
Basic information about this protein and its source genome.
- Accession
- PA2611
- Gene
- PA2611 cysG
- Status
- annotated
- Amino acids
- 465
- Structure source
- 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.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
9- GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
- GO:0043115 Catalysis of the reaction: NAD+ + precorrin-2 = 2 H+ + NADH + sirohydrochlorin.
- GO:0051266 Catalysis of the reaction: siroheme + 2 H+ = Fe(2+) + sirohydrochlorin.
- GO:0004851 Catalysis of the reaction: uroporphyrinogen III + 2 S-adenosyl-L-methionine = precorrin-2 + 2 S-adenosyl-L-homocysteine + H+.
- GO:0009236 The chemical reactions and pathways resulting in the formation of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
- GO:0032259 The process in which a methyl group is covalently attached to a molecule.
- GO:0019354 The chemical reactions and pathways resulting in the formation of siroheme, a tetrahydroporphyrin with adjacent, reduced pyrrole rings.
- GO:0008168 Catalysis of the transfer of a methyl group to an acceptor molecule.
- GO:0006779 The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 191 | 452 | PANTHER | PTHR45790 | SIROHEME SYNTHASE-RELATED |
| 1 | 465 | PIRSF | PIRSF036426 | Sirohaem_synth |
| 1 | 465 | InterPro | IPR012409 | Sirohaem synthase |
| 150 | 208 | Gene3D | G3DSA:1.10.8.210 | Sirohaem synthase, dimerisation domain |
| 150 | 208 | InterPro | IPR037115 | Sirohaem synthase, dimerisation domain superfamily |
| 213 | 332 | FunFam | G3DSA:3.40.1010.10:FF:000001 | Siroheme synthase |
| 297 | 330 | ProSitePatterns | PS00840 | Uroporphyrin-III C-methyltransferase signature 2. |
| 297 | 330 | InterPro | IPR003043 | Uroporphiryn-III C-methyltransferase, conserved site |
| 113 | 148 | Gene3D | G3DSA:3.30.160.110 | Siroheme synthase; domain 2 |
| 4 | 207 | NCBIfam | TIGR01470 | siroheme synthase, N-terminal domain |
| 4 | 207 | InterPro | IPR006367 | Sirohaem synthase, N-terminal |
| 214 | 459 | SUPERFAMILY | SSF53790 | Tetrapyrrole methylase |
| 214 | 459 | InterPro | IPR035996 | Tetrapyrrole methylase superfamily |
| 1 | 112 | Gene3D | G3DSA:3.40.50.720 | - |
| 6 | 115 | Pfam | PF13241 | Putative NAD(P)-binding |
| 114 | 210 | SUPERFAMILY | SSF75615 | Siroheme synthase middle domains-like |
| 1 | 113 | SUPERFAMILY | SSF51735 | NAD(P)-binding Rossmann-fold domains |
| 1 | 113 | InterPro | IPR036291 | NAD(P)-binding domain superfamily |
| 219 | 428 | Pfam | PF00590 | Tetrapyrrole (Corrin/Porphyrin) Methylases |
| 219 | 428 | InterPro | IPR000878 | Tetrapyrrole methylase |
| 1 | 461 | Hamap | MF_01646 | Siroheme synthase [cysG]. |
| 1 | 461 | InterPro | IPR012409 | Sirohaem synthase |
| 333 | 465 | FunFam | G3DSA:3.30.950.10:FF:000001 | Siroheme synthase |
| 217 | 452 | NCBIfam | TIGR01469 | uroporphyrinogen-III C-methyltransferase |
| 217 | 452 | InterPro | IPR006366 | Uroporphyrin-III C-methyltransferase |
| 333 | 465 | Gene3D | G3DSA:3.30.950.10 | - |
| 333 | 465 | InterPro | IPR014776 | Tetrapyrrole methylase, subdomain 2 |
| 151 | 207 | Pfam | PF10414 | Sirohaem synthase dimerisation region |
| 151 | 207 | InterPro | IPR019478 | Sirohaem synthase, dimerisation domain |
| 113 | 148 | FunFam | G3DSA:3.30.160.110:FF:000001 | Siroheme synthase |
| 222 | 449 | CDD | cd11642 | SUMT |
| 222 | 449 | InterPro | IPR006366 | Uroporphyrin-III C-methyltransferase |
| 209 | 332 | Gene3D | G3DSA:3.40.1010.10 | - |
| 209 | 332 | InterPro | IPR014777 | Tetrapyrrole methylase, subdomain 1 |
| 120 | 144 | Pfam | PF14824 | Sirohaem biosynthesis protein central |
| 120 | 144 | InterPro | IPR028281 | Siroheme synthase, central domain |
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...
Structural evidence
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA2611
|
AlphaFold | — | — | full sequence | — | Viewing |
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 |
|---|---|---|---|---|---|---|---|
| 2 | 0.829 | ||||||
| 1 | 0.734 |
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.
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 |
|---|---|---|---|---|---|---|
| FLC | Q5SKH6 | 189.1 Da LogP -5.25 TPSA 140.6 | ✓ Ro5 | ✓ Clean |
C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
|
|
| PQ2 | P25924 | 864.9 Da LogP 3.78 TPSA 354.4 | 2 viol. | ✓ Clean |
CC\1(C(/C/2=C/C3=N/C(=C\c4c(c(c([nH]4)Cc5c(c(c(…
|
|
| SHN | P25924 | 862.8 Da LogP 4.69 TPSA 355.8 | 2 viol. | ✓ Clean |
CC1(/c/2c/c3n/c(c\c4c(c(c([nH]4)cc5nc(/cc(\[nH]…
|
|
| UP2 | P95417 | 836.8 Da LogP 2.25 TPSA 361.6 | 2 viol. | ✓ Clean |
C1c2c(c(c([nH]2)Cc3c(c(c([nH]3)Cc4c(c(c([nH]4)C…
|
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.