MolNFT v1 · #27192 · protein

Crystal structure of P28L/Y173F tryptophan synthase alpha-subunits from escherichia COLI

1XCF · Tryptophan synthase alpha chain: “Crystal structure of P28L/Y173F tryptophan synthase alpha-subunits from escherichia COLI”. X-ray diffraction, 9 pockets (best druggability 0.67). MolNFT v1 #27192 on GenesisL1: 3D structure, binding…

PDB: 1XCF
Type: protein
Length: 476 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tryptophan synthase alpha chain
EC: 4.2.1.20
UniProt: P0A877
Pockets: 9 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Tryptophan synthase alpha chain (EC 4.2.1.20)	protein	238	51% helix, 15% strand	P0A877

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.67	0.93	25	empty
2	69	0.53	0.86	18	empty
3	50	0.53	0.88	17	empty
4	50	0.37	0.80	11	empty
5	109	0.37	0.74	17	empty

Interfaces

1 interface between chains.

A–B · 571 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

1XCF · Crystal structure of P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
P0A877 · AlphaFold monomer V2.0 prediction for tryptophan synthase alpha chain (P0A877) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P0A877
Elsewhere: RCSB PDB 1XCF · PDBe 1XCF · UniProt P0A877

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.