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Solution structure of peptidyl-prolyl cis-trans isomerase from burkholderia pseudomallei complexed with 1-{[(4-methylphenyl) THIO]ACETYL}PIPERIDINE

Analyse Solution structure of peptidyl-prolyl cis-trans isomerase from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2L2S
Type: protein
Length: 117 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase
EC: 5.2.1.8
UniProt: Q3JK38
Ligands: L2S
Pockets: 1 · best druggability 0.30

Structure

solution nmr · 1 distinct chain · 11% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8)	protein	117	11% helix, 37% strand	Q3JK38

Ligands and binding sites

L2S · 1-{[(4-methylphenyl)sulfanyl]acetyl}piperidine · 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	61	0.30	0.73	12	empty

Compared structures

2L2S · Solution structure of peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q3JK38
Elsewhere: RCSB PDB 2L2S · PDBe 2L2S · UniProt Q3JK38

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