MolNFT v1 · #52931 · protein

Atomic resolution crystal structure of the ppiase domain of human cyclophilin G

2WFI · Peptidyl-prolyl cis-trans isomerase G: “Atomic resolution crystal structure of the ppiase domain of human cyclophilin G”. X-ray diffraction, 1 ligand (MG), 1 pocket (best druggability 0.38). MolNFT v1 #52931 on GenesisL1: 3D…

PDB: 2WFI
Type: protein
Length: 172 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase G
EC: 5.2.1.8
UniProt: Q13427
Ligands: MG
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase G (EC 5.2.1.8)	protein	172	13% helix, 33% strand	Q13427

Ligands and binding sites

MG · Magnesium 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	88	0.38	0.76	26	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

2WFI · Atomic resolution crystal structure of the PPIase domain of human cyclophilin G · the same entry in another collection · chain A against A, TM-score 1.00
Q13427 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase G (Q13427) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q13427
Elsewhere: RCSB PDB 2WFI · PDBe 2WFI · UniProt Q13427

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