Research workbench

FOLD Q98H

Analyse FOLD Q98H in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5O2A
Type: protein
Length: 1,139 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bifunctional protein fold
EC: 1.5.1.5, 3.5.4.9
UniProt: P24186
Pockets: 15 · best druggability 0.63

Structure

x-ray diffraction · 3 distinct chains · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional protein fold (EC 1.5.1.5, 3.5.4.9)	protein	285	44% helix, 16% strand	P24186
B, D	Bifunctional protein fold (EC 1.5.1.5, 3.5.4.9)	protein	285	43% helix, 16% strand	P24186
C	Bifunctional protein fold (EC 1.5.1.5, 3.5.4.9)	protein	284	43% helix, 16% strand	P24186

Pockets

15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	389	0.63	0.78	38	empty
2	400	0.62	0.77	53	empty
3	277	0.62	0.79	42	empty
4	318	0.59	0.77	42	empty
5	276	0.58	0.77	30	empty

Interfaces

5 interfaces between chains.

A–B · 1678 Å² buried · 30 hydrogen bonds · protein-protein
C–D · 1507 Å² buried · 25 hydrogen bonds · protein-protein
B–C · 263 Å² buried · 1 hydrogen bond · protein-protein
B–D · 199 Å² buried · 3 hydrogen bonds · protein-protein
A–D · 45 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (methylation).

Compared structures

5O2A · FolD Q98H · the same entry in another collection · chain D against D, TM-score 1.00
P24186 · AlphaFold monomer V2.0 prediction for bifunctional protein fold (P24186) · a predicted model of the same protein · chain B against A, TM-score 0.96

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 P24186
Elsewhere: RCSB PDB 5O2A · PDBe 5O2A · UniProt P24186

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