MolNFT v1 · #82119 · protein

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

3VCP · Ring-hydroxylating dioxygenase: “The 2.2 ångström structure of STC2 with proline bound in the active site”. X-ray diffraction, 3 ligands (FES, PRO, FE), 3 pockets (best druggability 0.77). MolNFT v1 #82119 on GenesisL1: 3D…

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

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