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Crystal structure analysis of O-acetylserine sulfhydrylase CYSK2 complexed with cystine from microcystis aeruginosa 7806

Analyse Crystal structure analysis of O-acetylserine sulfhydrylase CYSK2 complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LMB
Type: protein
Length: 310 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cysteine synthase
EC: 2.5.1.47
UniProt: A8YBP8
Ligands: CYS, PLP
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cysteine synthase (EC 2.5.1.47)	protein	310	43% helix, 18% strand	A8YBP8

Ligands and binding sites

CYS · Cysteine · ligand · 2 copies · chains A
PLP · Pyridoxal-5'-phosphate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	69	0.74	0.98	26	PLP
2	207	0.58	0.80	41	CYS
3	58	0.38	0.80	12	empty

Modifications

Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).

Compared structures

4LMB · Crystal structure analysis of O-acetylserine sulfhydrylase CysK2 complexed with cystine… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A8YBP8
Elsewhere: RCSB PDB 4LMB · PDBe 4LMB · UniProt A8YBP8

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