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L-tryptophan aminotransferase

Analyse L-tryptophan aminotransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BWO
Type: protein
Length: 2,171 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-tryptophan aminotransferase
UniProt: Q9S7N2
Pockets: 17 · best druggability 0.61

Structure

x-ray diffraction · 6 distinct chains · 37% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-tryptophan aminotransferase	protein	363	37% helix, 19% strand	Q9S7N2
B	L-tryptophan aminotransferase	protein	364	37% helix, 18% strand	Q9S7N2
C	L-tryptophan aminotransferase	protein	360	38% helix, 18% strand	Q9S7N2
D	L-tryptophan aminotransferase	protein	360	36% helix, 18% strand	Q9S7N2
E	L-tryptophan aminotransferase	protein	361	35% helix, 19% strand	Q9S7N2
F	L-tryptophan aminotransferase	protein	363	36% helix, 20% strand	Q9S7N2

Pockets

17 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	220	0.61	0.81	23	empty
2	218	0.61	0.81	24	empty
3	252	0.60	0.79	33	empty
4	218	0.60	0.81	25	empty
5	224	0.59	0.80	25	empty

Interfaces

5 interfaces between chains.

C–D · 2511 Å² buried · 58 hydrogen bonds · protein-protein
A–B · 2487 Å² buried · 66 hydrogen bonds · protein-protein
E–F · 2483 Å² buried · 58 hydrogen bonds · protein-protein
A–F · 236 Å² buried · 0 hydrogen bonds · protein-protein
A–D · 116 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (cofactor).

Compared structures

3BWO · L-tryptophan aminotransferase · the same entry in another collection · chain F against F, TM-score 1.00
Q9S7N2 · AlphaFold monomer V2.0 prediction for L-tryptophan--pyruvate aminotransferase 1 (Q9S7N2) · a predicted model of the same protein · chain E 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 Q9S7N2
Elsewhere: RCSB PDB 3BWO · PDBe 3BWO · UniProt Q9S7N2

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