MolNFT v1 · #91928 · protein

Crystal structure of mutated cyclophilin B that causes hyperelastosis cutis in the american quarter horse

4FRV · Peptidyl-prolyl cis-trans isomerase: “Crystal structure of mutated cyclophilin B that causes hyperelastosis cutis in the american quarter horse”. X-ray diffraction, 2 ligands (ME2, ZN), 1 pocket (best druggability 0.37). MolNFT v1…

PDB: 4FRV
Type: protein
Length: 185 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase
EC: 5.2.1.8
UniProt: A5YBL8
Ligands: ME2, ZN
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8)	protein	185	12% helix, 36% strand	A5YBL8

Ligands and binding sites

ME2 · 1-ethoxy-2-(2-methoxyethoxy)ethane · ligand · chains A
ZN · Zinc ion · metal · 2 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 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	86	0.37	0.76	22	empty

Compared structures

4FRV · Crystal structure of mutated cyclophilin B that causes hyperelastosis cutis in the… · the same entry in another collection · chain A against A, TM-score 1.00

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 A5YBL8
Elsewhere: RCSB PDB 4FRV · PDBe 4FRV · UniProt A5YBL8

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