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Crystal structure of a fungal L-serine ammonia-lyase from rhizomucor miehei

Analyse Crystal structure of a fungal L-serine ammonia-lyase from rhizomucor miehei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5C3U
Type: protein
Length: 315 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-serine ammonia-lyase
EC: 4.3.1.17
Ligands: PLP
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-serine ammonia-lyase (EC 4.3.1.17)	protein	315	48% helix, 16% strand	—

Ligands and binding sites

PLP · Pyridoxal-5'-phosphate · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	360	0.68	0.82	62	PLP

Modifications

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

Compared structures

5C3U · Crystal structure of a fungal L-serine ammonia-lyase from Rhizomucor miehei · 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
Elsewhere: RCSB PDB 5C3U · PDBe 5C3U

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