MolNFT v1 · #46954 · protein

X-ray structure of human cyclophilin J at 2.0 ångström

2OK3 · Peptidyl-prolyl cis-trans isomerase-like 3: “X-ray structure of human cyclophilin J at 2.0 ångström”. X-ray diffraction, 1 ligand (NI), 1 pocket (best druggability 0.35). MolNFT v1 #46954 on GenesisL1: 3D structure, binding sites…

PDB: 2OK3
Type: protein
Length: 160 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase-like 3
EC: 5.2.1.8
UniProt: Q9H2H8
Ligands: NI
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase-like 3 (EC 5.2.1.8)	protein	160	14% helix, 30% strand	Q9H2H8

Ligands and binding sites

NI · Nickel (II) ion · metal · 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	59	0.35	0.78	21	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2OK3 · X-ray structure of human cyclophilin J at 2.0 angstrom · the same entry in another collection · chain A against A, TM-score 1.00
Q9H2H8 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase-like 3 (Q9H2H8) · 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 Q9H2H8
Elsewhere: RCSB PDB 2OK3 · PDBe 2OK3 · UniProt Q9H2H8

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