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Escherichia COLI tryptophanase in holo form

Analyse Escherichia COLI tryptophanase in holo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4W4H
Type: protein
Length: 861 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tryptophanase
EC: 4.1.99.1
UniProt: P0A853
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tryptophanase (EC 4.1.99.1)	protein	428	47% helix, 14% strand	P0A853
B	Tryptophanase (EC 4.1.99.1)	protein	433	47% helix, 14% strand	P0A853

Pockets

4 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	348	0.61	0.78	44	empty
2	313	0.59	0.78	35	empty
3	76	0.34	0.75	16	empty
4	65	0.31	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 1944 Å² buried · 40 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (cofactor).

Compared structures

4W4H · Escherichia coli tryptophanase in holo form · the same entry in another collection · chain A against A, TM-score 1.00
P0A853 · AlphaFold monomer V2.0 prediction for tryptophanase (P0A853) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P0A853
Elsewhere: RCSB PDB 4W4H · PDBe 4W4H · UniProt P0A853

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