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Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from escherichia COLI refined at 2.0 ångströms resolution

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

PDB: 1PII
Type: protein
Length: 452 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-(5'PHOSPHORIBOSYL)ANTHRANILATE isomerase
EC: 4.1.1.48
UniProt: P00909
Ligands: PO4
Pockets: 4 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-(5'PHOSPHORIBOSYL)ANTHRANILATE isomerase (EC 4.1.1.48)	protein	452	38% helix, 20% strand	P00909

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	131	0.75	0.94	29	PO4
2	150	0.68	0.89	28	PO4
3	97	0.34	0.74	23	empty
4	53	0.31	0.77	16	empty

Compared structures

1PII · Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate… · 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 0.99

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Every structure of UniProt P00909
Elsewhere: RCSB PDB 1PII · PDBe 1PII · UniProt P00909

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