Research workbench

The 2.2 ångström structure of STC2 with proline bound in the active site

Analyse The 2.2 ångström structure of STC2 with proline bound in the active site in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VCP
Type: protein
Length: 397 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ring-hydroxylating dioxygenase
UniProt: Q92ZP9
Ligands: FES, PRO, FE
Pockets: 3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ring-hydroxylating dioxygenase	protein	397	30% helix, 26% strand	Q92ZP9

Ligands and binding sites

FES · Fe2/s2 (inorganic) cluster · ligand · chains A
PRO · Proline · ligand · chains A
FE · Fe (III) ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	87	0.77	0.98	29	PRO
2	134	0.46	0.77	20	empty
3	50	0.30	0.76	17	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3VCP · The 2.2 Angstrom structure of Stc2 with proline bound in the active site · 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 Q92ZP9
Elsewhere: RCSB PDB 3VCP · PDBe 3VCP · UniProt Q92ZP9

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.