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Bacterial cystathionine gamma-lyase mccb of staphylococcus aureus with cofactor plp

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

PDB: 6KHQ
Type: protein
Length: 740 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cystathionine gamma lyase
EC: 4.4.1.1
UniProt: A0A0H3JQ19
Pockets: 6 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cystathionine gamma lyase (EC 4.4.1.1)	protein	364	39% helix, 18% strand	A0A0H3JQ19
B	Cystathionine gamma lyase (EC 4.4.1.1)	protein	376	39% helix, 16% strand	A0A0H3JQ19

Pockets

6 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	74	0.47	0.83	25	empty
2	167	0.47	0.76	21	empty
3	109	0.39	0.75	20	empty
4	114	0.38	0.74	19	empty
5	55	0.33	0.77	13	empty

Interfaces

1 interface between chains.

A–B · 1589 Å² buried · 28 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (cofactor).

Compared structures

6KHQ · bacterial cystathionine gamma-lyase MccB of Staphylococcus aureus with cofactor PLP · 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 6KHQ · PDBe 6KHQ · UniProt A0A0H3JQ19

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