MolNFT v1 · #153081 · protein

Crystal structure of ATFKBP53 C-terminal domain

6J2M · Peptidyl-prolyl cis-trans isomerase FKBP53: “Crystal structure of ATFKBP53 C-terminal domain”. X-ray diffraction, 2 ligands (FK5, CL), 1 pocket (best druggability 0.34). MolNFT v1 #153081 on GenesisL1: 3D structure, binding sites…

PDB: 6J2M
Type: protein
Length: 111 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase FKBP53
EC: 5.2.1.8
UniProt: Q93ZG9
Ligands: FK5, CL
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase FKBP53 (EC 5.2.1.8)	protein	111	9% helix, 40% strand	Q93ZG9

Ligands and binding sites

FK5 · 8-deethyl-8-[but-3-enyl]-ascomycin · ligand · chains A
CL · Chloride ion · ion · 14 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	60	0.34	0.76	14	empty

Compared structures

6J2M · Crystal structure of AtFKBP53 C-terminal domain · the same entry in another collection · chain A against A, TM-score 1.00
Q93ZG9 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP53 (Q93ZG9) · 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 Q93ZG9
Elsewhere: RCSB PDB 6J2M · PDBe 6J2M · UniProt Q93ZG9

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