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Alternative models for two crystal structures of candida albicans 3,4-dihydroxy-2-butanone 4-phosphate synthase- alternate interpreation

Analyse Alternative models for two crystal structures of candida albicans… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2RIU
Type: protein
Length: 195 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3,4-dihydroxy-2-butanone 4-phosphate synthase
UniProt: Q5A3V6
Ligands: 5RP
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3,4-dihydroxy-2-butanone 4-phosphate synthase	protein	195	38% helix, 24% strand	Q5A3V6

Ligands and binding sites

5RP · Ribulose-5-phosphate · ligand · chains A

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

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	51	0.30	0.76	13	5RP

Compared structures

2RIU · Alternative models for two crystal structures of Candida albicans 3,4-dihydroxy-2-buta… · the same entry in another collection · chain A against A, TM-score 1.00
Q5A3V6 · AlphaFold monomer V2.0 prediction for 3,4-dihydroxy-2-butanone 4-phosphate synthase… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q5A3V6
Elsewhere: RCSB PDB 2RIU · PDBe 2RIU · UniProt Q5A3V6

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