MolNFT v1 · #72719 · protein

Crystal structure of bifunctional 5,10-methylenetetrahydrofolate dehydrogenase / cyclohydrolase from thermoplasma acidophilum

3NGX · Bifunctional protein fold: “Crystal structure of bifunctional 5,10-methylenetetrahydrofolate dehydrogenase / cyclohydrolase from…”. X-ray diffraction, 4 pockets (best druggability 0.65). MolNFT v1 #72719 on GenesisL1: 3D structure…

PDB: 3NGX
Type: protein
Length: 550 residues
Chains: 2
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: Q05213
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Bifunctional protein fold (EC 1.5.1.5, 3.5.4.9)	protein	275	45% helix, 17% strand	Q05213

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	462	0.65	0.77	45	empty
2	464	0.62	0.76	45	empty
3	98	0.42	0.78	29	empty
4	83	0.34	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 1574 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

3NGX · Crystal structure of bifunctional 5,10-methylenetetrahydrofolate dehydrogenase /… · the same entry in another collection · chain A against A, TM-score 1.00
Q05213 · AlphaFold monomer V2.0 prediction for bifunctional protein fold (Q05213) · a predicted model of the same protein · 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 Q05213
Elsewhere: RCSB PDB 3NGX · PDBe 3NGX · UniProt Q05213

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