Research workbench

bacterial cystathionine gamma-lyase MccB of Staphylococcus aureus

Analyse bacterial cystathionine gamma-lyase MccB of Staphylococcus aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KGZ
Type: protein
Length: 368 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.3
Source: Staphylococcus aureus subsp. aureus Mu50
Molecule: Cystathionine gamma-lyase
EC: 4.4.1.1
UniProt: A0A0H3JQ19
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · resolution 2.3 · 1 distinct chain · 40% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cystathionine gamma-lyase (EC 4.4.1.1)	protein	368	40% helix, 15% strand	A0A0H3JQ19

Ligands and binding sites

TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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	307	0.67	0.82	36	TRS
2	62	0.41	0.81	14	empty

Compared structures

6KGZ · Bacterial cystathionine gamma-lyase mccb of staphylococcus aureus · the same entry in another collection · chain A against A, TM-score 1.00

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 A0A0H3JQ19
Elsewhere: RCSB PDB 6KGZ · PDBe 6KGZ · UniProt A0A0H3JQ19

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