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Crystal structure of the ppiase-chaperone slpa with the chaperone binding site occupied by the linker of the purification tag

Analyse Crystal structure of the ppiase-chaperone slpa with the chaperone binding site… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DT4
Type: protein
Length: 160 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fkbp-type 16 kda peptidyl-prolyl cis-trans isomerase
EC: 5.2.1.8
UniProt: P0AEM0
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fkbp-type 16 kda peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8)	protein	160	13% helix, 37% strand	P0AEM0

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	76	0.32	0.73	14	empty

Compared structures

4DT4 · Crystal structure of the PPIase-chaperone SlpA with the chaperone binding site occupied… · the same entry in another collection · chain A against A, TM-score 1.00
P0AEM0 · AlphaFold monomer V2.0 prediction for fkbp-type 16 kda peptidyl- prolyl cis-trans… · a predicted model of the same protein · chain A against A, TM-score 0.76

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 P0AEM0
Elsewhere: RCSB PDB 4DT4 · PDBe 4DT4 · UniProt P0AEM0

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