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Crystal structure of hydrogen sulfide-producing enzyme (FN1055) from fusobacterium nucleatum

Analyse Crystal structure of hydrogen sulfide-producing enzyme (FN1055) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5B53
Type: protein
Length: 334 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cysteine synthase
EC: 2.5.1.47
UniProt: Q8REP3
Ligands: PLP, CL
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cysteine synthase (EC 2.5.1.47)	protein	334	42% helix, 19% strand	Q8REP3

Ligands and binding sites

PLP · Pyridoxal-5'-phosphate · ligand · chains A
CL · Chloride ion · ion · 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	52	0.69	0.98	21	PLP
2	423	0.68	0.80	40	empty
3	89	0.42	0.78	14	empty

Modifications

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

Compared structures

5B53 · Crystal structure of hydrogen sulfide-producing enzyme (Fn1055) from Fusobacterium… · 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 Q8REP3
Elsewhere: RCSB PDB 5B53 · PDBe 5B53 · UniProt Q8REP3

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