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C-terminal domain of fission yeast OFD1

Analyse C-terminal domain of fission yeast OFD1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6E0T
Type: protein
Length: 248 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prolyl 3,4-dihydroxylase OFD1
EC: 1.14.11.-
UniProt: Q11120
Pockets: 2 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Prolyl 3,4-dihydroxylase OFD1 (EC 1.14.11.-)	protein	248	25% helix, 29% strand	Q11120

Pockets

2 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	254	0.58	0.79	27	empty
2	88	0.41	0.78	18	empty

Compared structures

6E0T · C-terminal domain of Fission Yeast OFD1 · the same entry in another collection · chain X against X, TM-score 1.00
Q11120 · AlphaFold monomer V2.0 prediction for prolyl 3,4-dihydroxylase OFD1 (Q11120) · a predicted model of the same protein · chain X against A, TM-score 0.97

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 Q11120
Elsewhere: RCSB PDB 6E0T · PDBe 6E0T · UniProt Q11120

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