MolNFT v1 · #60061 · protein

Crystal structure of thermophilic slyd

3CGM · Peptidyl-prolyl cis-trans isomerase: “Crystal structure of thermophilic slyd”. X-ray diffraction, 2 ligands (NI, SCN), 1 pocket (best druggability 0.34). MolNFT v1 #60061 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3CGM
Type: protein
Length: 157 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: Q5SLE7
Ligands: NI, SCN
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8)	protein	157	14% helix, 44% strand	Q5SLE7

Ligands and binding sites

NI · Nickel (II) ion · metal · chains A
SCN · Thiocyanate ion · ion · 6 copies · chains A
GOL · Glycerol · additive · 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	63	0.34	0.76	14	SCN

Compared structures

3CGM · Crystal structure of thermophilic SlyD · 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 Q5SLE7
Elsewhere: RCSB PDB 3CGM · PDBe 3CGM · UniProt Q5SLE7

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