Research workbench

Propionibacterium shermanii transcarboxylase 5S subunit A59T

Analyse Propionibacterium shermanii transcarboxylase 5S subunit A59T in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1S3H
Type: protein
Length: 472 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcarboxylase 5S subunit
EC: 2.1.3.1
UniProt: Q70AC7
Ligands: CO
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcarboxylase 5S subunit (EC 2.1.3.1)	protein	472	51% helix, 11% strand	Q70AC7

Ligands and binding sites

CO · Cobalt (II) ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	616	0.69	0.78	68	empty
2	112	0.45	0.79	16	empty

Modifications

Observed in the structure: 1 modified (carboxylation).

Compared structures

1S3H · Propionibacterium shermanii transcarboxylase 5S subunit A59T · the same entry in another collection · chain A against A, TM-score 1.00
Q70AC7 · AlphaFold monomer V2.0 prediction for methylmalonyl-CoA carboxyltransferase 5S subunit… · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q70AC7
Elsewhere: RCSB PDB 1S3H · PDBe 1S3H · UniProt Q70AC7

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