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Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis (Y78F-C503S-C565S) bound to cinnamate

Analyse Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LTM
Type: protein
Length: 1,074 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phenylalanine ammonia lyase
Ligands: HCI
Pockets: 12 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Phenylalanine ammonia lyase	protein	537	56% helix, 6% strand	—

Ligands and binding sites

HCI · Hydrocinnamic acid · ligand · 2 copies · chains B, A

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

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	56	0.71	0.98	22	empty
2	93	0.61	0.88	25	empty
3	191	0.60	0.82	36	HCI
4	182	0.59	0.81	34	HCI
5	200	0.56	0.80	35	empty

Interfaces

1 interface between chains.

B–A · 4048 Å² buried · 64 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (nonstandard).

Compared structures

5LTM · Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis… · 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 5LTM · PDBe 5LTM

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