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Three-dimensional structure of a truncated phosphoribosylanthranilate isomerase (residues 255-384) from escherichia COLI

Analyse Three-dimensional structure of a truncated phosphoribosylanthranilate isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2KZH
Type: protein
Length: 134 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tryptophan biosynthesis protein trpcf
EC: 5.3.1.24
UniProt: P00909
Pockets: 1 · best druggability 0.36

Structure

solution nmr · 1 distinct chain · 31% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tryptophan biosynthesis protein trpcf (EC 5.3.1.24)	protein	134	31% helix, 17% strand	P00909

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	87	0.36	0.75	17	empty

Compared structures

2KZH · Three-dimensional structure of a truncated phosphoribosylanthranilate isomerase (residues… · the same entry in another collection · chain A against A, TM-score 1.00
P00909 · AlphaFold monomer V2.0 prediction for tryptophan biosynthesis protein trpcf (P00909) · a predicted model of the same protein · chain A against A, TM-score 0.75

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 P00909
Elsewhere: RCSB PDB 2KZH · PDBe 2KZH · UniProt P00909

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