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Crystal structure of pria from actinomyces urogenitalis

Analyse Crystal structure of pria from actinomyces urogenitalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4X2R
Type: protein
Length: 243 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino) methylideneamino] imidazole-4-carboxamide…
EC: 5.3.1.16
UniProt: C0W7K4
Ligands: PO4
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino) methylideneamino] imidazole-4-carboxamide isomerase (EC 5.3.1.16)	protein	243	42% helix, 23% strand	C0W7K4

Ligands and binding sites

PO4 · Phosphate ion · ion · 4 copies · chains A
CXS · 3-cyclohexyl-1-propylsulfonic acid · additive · chains A

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

Pockets

2 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	199	0.76	0.92	48	PO4
2	93	0.56	0.85	19	empty

Compared structures

4X2R · Crystal structure of PriA from Actinomyces urogenitalis · the same entry in another collection · chain A against A, TM-score 1.00

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 C0W7K4
Elsewhere: RCSB PDB 4X2R · PDBe 4X2R · UniProt C0W7K4

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