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Structural analysis of protein folding by the methanococcus jannaschii chaperone FKBP26

Analyse Structural analysis of protein folding by the methanococcus jannaschii… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PRA
Type: protein
Length: 300 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fkbp-type peptidyl-prolyl cis-trans isomerase
EC: 5.2.1.8
UniProt: Q58235
Pockets: 2 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Fkbp-type peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8)	protein	150	17% helix, 35% strand	Q58235

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	72	0.29	0.73	20	empty
2	62	0.28	0.73	20	empty

Interfaces

1 interface between chains.

A–B · 983 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

3PRA · Structural analysis of protein folding by the Methanococcus jannaschii chaperone FKBP26 · the same entry in another collection · chain A against A, TM-score 1.00
Q58235 · AlphaFold monomer V2.0 prediction for long-type peptidyl-prolyl cis- trans isomerase… · 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 Q58235
Elsewhere: RCSB PDB 3PRA · PDBe 3PRA · UniProt Q58235

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