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Crystal structure of staphylococcus aureus cystathionine gamma lyase holoenzyme Y103A mutant

Analyse Crystal structure of staphylococcus aureus cystathionine gamma lyase holoenzyme… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MD9
Type: protein
Length: 380 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bifunctional cystathionine gamma-LYASE/HOMOCYSTEINE desulfhydrase
EC: 4.4.1.1, 4.4.1.8, 2.5.1.48
UniProt: X5E0F1
Ligands: NA
Pockets: 2 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	Bifunctional cystathionine gamma-LYASE/HOMOCYSTEINE desulfhydrase (EC 4.4.1.1, 4.4.1.8, 2.5.1.48)	protein	380	41% helix, 17% strand	X5E0F1

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains H

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	176	0.48	0.76	27	empty
2	117	0.40	0.75	19	empty

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

7MD9 · Crystal structure of Staphylococcus aureus cystathionine gamma lyase holoenzyme Y103A… · the same entry in another collection · chain H against H, 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 X5E0F1
Elsewhere: RCSB PDB 7MD9 · PDBe 7MD9 · UniProt X5E0F1

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