MolNFT v1 · #105575 · protein

Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with formate

4R8V: “Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with…”. X-ray diffraction, 1 pocket (best druggability 0.63). MolNFT v1 #105575 on GenesisL1: 3D structure, binding sites and…

PDB: 4R8V
Type: protein
Length: 308 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 10-formyltetrahydrofolate dehydrogenase
EC: 1.5.1.6
UniProt: E3NZ06
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	10-formyltetrahydrofolate dehydrogenase (EC 1.5.1.6)	protein	308	27% helix, 28% strand	E3NZ06

Ligands and binding sites

BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A
FMT · Formic acid · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	387	0.63	0.78	36	BTB, PEG, FMT

Compared structures

4R8V · Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase… · 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 E3NZ06
Elsewhere: RCSB PDB 4R8V · PDBe 4R8V · UniProt E3NZ06

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