MolNFT v1 · #22488 · protein

Crystal structure of phenylalanine ammonia lyase from rhodosporidium toruloides

1T6P · Phenylalanine ammonia-lyase: “Crystal structure of phenylalanine ammonia lyase from rhodosporidium toruloides”. X-ray diffraction, 20 pockets (best druggability 0.83). MolNFT v1 #22488 on GenesisL1: 3D structure, binding sites and…

PDB: 1T6P
Type: protein
Length: 5,219 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phenylalanine ammonia-lyase
EC: 4.3.1.5
UniProt: P11544
Pockets: 20 · best druggability 0.83

Structure

x-ray diffraction · 8 distinct chains · 59% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phenylalanine ammonia-lyase (EC 4.3.1.5)	protein	654	59% helix, 5% strand	P11544
B	Phenylalanine ammonia-lyase (EC 4.3.1.5)	protein	660	59% helix, 5% strand	P11544
C	Phenylalanine ammonia-lyase (EC 4.3.1.5)	protein	650	59% helix, 5% strand	P11544
D	Phenylalanine ammonia-lyase (EC 4.3.1.5)	protein	650	59% helix, 5% strand	P11544
E	Phenylalanine ammonia-lyase (EC 4.3.1.5)	protein	655	59% helix, 4% strand	P11544
F	Phenylalanine ammonia-lyase (EC 4.3.1.5)	protein	650	59% helix, 5% strand	P11544
G	Phenylalanine ammonia-lyase (EC 4.3.1.5)	protein	656	60% helix, 4% strand	P11544
H	Phenylalanine ammonia-lyase (EC 4.3.1.5)	protein	644	59% helix, 5% strand	P11544

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1064	0.83	0.84	107	empty
2	967	0.82	0.84	92	empty
3	856	0.81	0.84	77	empty
4	823	0.81	0.84	70	empty
5	200	0.79	0.93	28	empty

Interfaces

14 interfaces between chains.

B–C · 4446 Å² buried · 62 hydrogen bonds · protein-protein
A–D · 4435 Å² buried · 64 hydrogen bonds · protein-protein
F–H · 4397 Å² buried · 67 hydrogen bonds · protein-protein
E–G · 4367 Å² buried · 60 hydrogen bonds · protein-protein
F–G · 3313 Å² buried · 40 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 112 modified (engineered, nonstandard).

Compared structures

1T6P · Crystal Structure of Phenylalanine Ammonia Lyase from Rhodosporidium toruloides · the same entry in another collection · chain B against B, TM-score 1.00
P11544 · AlphaFold monomer V2.0 prediction for PHENYLALANINE/TYROSINE ammonia- lyase (P11544) · a predicted model of the same protein · chain H against A, TM-score 0.99

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 P11544
Elsewhere: RCSB PDB 1T6P · PDBe 1T6P · UniProt P11544

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