MolNFT v1 · #55023 · protein

Crystal structure of BPSS1823, a mip-like chaperone from burkholderia pseudomallei

2Y78 · Peptidyl-prolyl cis-trans isomerase: “Crystal structure of BPSS1823, a mip-like chaperone from burkholderia pseudomallei”. X-ray diffraction, 2 ligands (SO4, CL), 1 pocket (best druggability 0.32). MolNFT v1 #55023 on GenesisL1: 3D…

PDB: 2Y78
Type: protein
Length: 122 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase
EC: 5.2.1.8
UniProt: Q63J95
Ligands: SO4, CL
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8)	protein	122	10% helix, 37% strand	Q63J95

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A
CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · 2 copies · 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	54	0.32	0.75	13	empty

Compared structures

2Y78 · Crystal structure of BPSS1823, a Mip-like chaperone from Burkholderia pseudomallei · 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 Q63J95
Elsewhere: RCSB PDB 2Y78 · PDBe 2Y78 · UniProt Q63J95

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